NCBI Conserved Domain Search

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1813-1855

9.31e-27

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: 104.25 E-value: 9.31e-27

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1813 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 1855
Cdd:cd15659      1 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 43

PHD2_NSD1

cd15650

PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1285-1331

5.44e-26

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: 102.27 E-value: 5.44e-26

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1285 TCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:cd15650      1 TCFVCKKSDEDVRRCMLPLCGKFYHEECVLKYPPTVMQNRGFRCSLH 47

PHD1_NSD1_2

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...

1238-1280

1.14e-22

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: 92.54 E-value: 1.14e-22

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1238 VCQNCEKLGELLLCEAQCCGAFHLECLGLTEMPRGKFICNECR 1280
Cdd:cd15648      1 VCQVCEKPGELLLCEGQCCGAFHLDCIGLSEMPSGKFICDECI 43

PHD4_NSD1

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1402-1441

1.15e-22

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: 92.39 E-value: 1.15e-22

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDC 1441
Cdd:cd15656      1 WCFVCSEGGSLLCCESCPAAFHRECLNIDMPEGSWYCNDC 40

C5HCH

pfam17982

NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family ...

1854-1903

9.88e-20

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: 84.44 E-value: 9.88e-20

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1854 WHQCDVCGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGP 1903
Cdd:pfam17982    1 WHQCSVCGSPATSFCEFCPSSFCKDHEKGALVPSALEGRLCCSEHDPESP 50

AWS

pfam17907

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...

1594-1632

3.44e-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: 65.52 E-value: 3.44e-13

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1594 DENPCGIDSECINRMLLYECHPTVCPAGGRCQNQCFSKR 1632
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39

PHA03247 super family

cl33720

large tegument protein UL36; Provisional

1916-2288

4.34e-09

large tegument protein UL36; Provisional

The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 62.65 E-value: 4.34e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1916 PPTATLSPSPGtqqteqssemgtqgPKKSDQPPTDATQMlslSKKAVTGTCQRPllpERPPERTDSSShlldrirdlagS 1995
Cdd:PHA03247  2553 PPLPPAAPPAA--------------PDRSVPPPRPAPRP---SEPAVTSRARRP---DAPPQSARPRA-----------P 2601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1996 GTKSQSLVSSQRPQDRPPAKEGPRPQPPDRASPVTRPSSSPSVSSLPLERPLRMTEP---RLDKSIGAASPKSQAVEKPP 2072
Cdd:PHA03247  2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQ 2681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2073 APTglRLSSPDRLLN-TNSPKPQISDRPPDKSHASLTQRLPPPEKVLSAVVQSLVAkekalrPVDQNTQAKHRAAVVmDL 2151
Cdd:PHA03247  2682 RPR--RRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAL------PAAPAPPAVPAGPAT-PG 2752

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2152 IDLTPRQKERAASPQEVTAQADEKTPVLESSSRPT----SRGLGHVPRAVEKGGVSDPLQPPGKSAAPSEHPWQAVKSLT 2227
Cdd:PHA03247  2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT 2832

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 2228 HARFLSPPSAKAFLYESAIQASGRAPVGSEQTPGPPSPAPGLLK-----QVKQLSRGLTAKSGQSF 2288
Cdd:PHA03247  2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAaparpPVRRLARPAVSRSTESF 2898

TNG2 super family

cl34876

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

1147-1280

1.33e-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: 43.00 E-value: 1.33e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1147 KEFGGGTTRIFDKPRKRKRqrhGTARVHYKRVKKEDSARETPSSAEGELmIHRTAASPKEILEEGIEHDPGMSASKRLQG 1226
Cdd:COG5034    144 EHRSAASSQGSRHTKLKKR---KNIHNLKRRSPELSSKREVSFTLESPS-VPDTATRVKEGNNGGSTKSRGVSSEDNSEG 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 1227 ERgggaalKENVCQNCEkLGELLLCEAQCCGA--FHLECLGLTEMPRGKFICNECR 1280
Cdd:COG5034    220 EE------LYCFCQQVS-YGQMVACDNANCKRewFHLECVGLKEPPKGKWYCPECK 268

Name

Accession

Description

Interval

E-value

SET_NSD1

cd19210

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...

1634-1775

2.12e-106

Pssm-ID: 380987 [Multi-domain] Cd Length: 142 Bit Score: 335.74 E-value: 2.12e-106

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1634 YPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 1713
Cdd:cd19210      1 YPEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498 1714 HCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1775
Cdd:cd19210     81 HCCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 142

PWWP_NSD1_rpt1

cd20161

first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...

13-128

2.65e-71

Pssm-ID: 438989 Cd Length: 116 Bit Score: 234.29 E-value: 2.65e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   13 PLKYEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVANRRPYREYYVEAFGDPSEKAWVAGKAIVMFEGRHQFEELPV 92
Cdd:cd20161      1 PVKYEVGDLVWAKFSRRPWWPCRICADPLLDTHSKMKVPSRRPCRQYYVETLGELTEKAWVAAKAVVPFEGRHQFEELPV 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958702498   93 LRKRGKQKEKGYRHKVPQKILSKWEASVGLAEQCDV 128
Cdd:cd20161     81 LRRRGKQKEKDYKHKIPQKLLSLWEASVAHAEDFLS 116

PWWP_NSD1_rpt2

cd20164

second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...

1448-1543

3.77e-69

Pssm-ID: 438992 Cd Length: 96 Bit Score: 227.07 E-value: 3.77e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1448 HYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 1527
Cdd:cd20164      1 HYKEVVWVKVGRYRWWPAEVCHPKSIPTNIQKMKHDIGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 80

                           90
                   ....*....|....*.
gi 1958702498 1528 KKALQEAAARFEELKA 1543
Cdd:cd20164     81 KKALQEAAVRFEELKA 96

SET

smart00317

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

1635-1758

2.79e-47

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: 165.59 E-value: 2.79e-47

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498  1635 PDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNH 1714
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1958702498  1715 CCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGN 1758
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

SET

COG2940

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

1635-1772

1.86e-32

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 123.92 E-value: 1.86e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1635 PDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItnfYMLTLDKDRIIDAGPKGNYARFMNH 1714
Cdd:COG2940      6 PRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT---YLFELDDDGVIDGALGGNPARFINH 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958702498 1715 CCQPNCETqkwsVNGDTRVGLFALSDIKAGTELTFNYNLEClGNGKTVCKCgaPNCSG 1772
Cdd:COG2940     83 SCDPNCEA----DEEDGRIFIVALRDIAAGEELTYDYGLDY-DEEEYPCRC--PNCRG 133

PHD3_NSD1

cd15653

PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1332-1385

1.46e-31

Pssm-ID: 277123 Cd Length: 54 Bit Score: 118.10 E-value: 1.46e-31

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958702498 1332 ICITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSKILASNSIICPNH 1385
Cdd:cd15653      1 ICLTCHATNPSNPSASKGRLMRCVRCPVAYHANDFCLAAGSVILASNSIICPNH 54

SET

pfam00856

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...

1646-1752

2.26e-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: 117.24 E-value: 2.26e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGE-LIDEEECRARIRYAQEHDIT---NFYMLTLDKD--RIID--AGPKGNYARFMNHCCQ 1717
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELrlwGPYLFTLDEDseYCIDarALYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958702498 1718 PNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYN 1752
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

PWWP

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...

1451-1539

2.52e-28

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: 110.21 E-value: 2.52e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDV--SSKDKMGKGVDGTYK 1528
Cdd:pfam00855    2 DLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEfeYLKKKKKKKKKKAFK 81

                           90
                   ....*....|.
gi 1958702498 1529 KALQEAAARFE 1539
Cdd:pfam00855   82 KALEEAEEALK 92

PHD5_NSD1

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1813-1855

9.31e-27

Pssm-ID: 277129 Cd Length: 43 Bit Score: 104.25 E-value: 9.31e-27

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1813 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 1855
Cdd:cd15659      1 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 43

PHD2_NSD1

cd15650

PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1285-1331

5.44e-26

Pssm-ID: 277120 Cd Length: 47 Bit Score: 102.27 E-value: 5.44e-26

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1285 TCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:cd15650      1 TCFVCKKSDEDVRRCMLPLCGKFYHEECVLKYPPTVMQNRGFRCSLH 47

PWWP

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

1447-1509

1.53e-25

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

Pssm-ID: 214603 [Multi-domain] Cd Length: 63 Bit Score: 101.27 E-value: 1.53e-25

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958702498  1447 PHYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYM 1509
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63

PHD1_NSD1_2

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...

1238-1280

1.14e-22

Pssm-ID: 277118 Cd Length: 43 Bit Score: 92.54 E-value: 1.14e-22

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1238 VCQNCEKLGELLLCEAQCCGAFHLECLGLTEMPRGKFICNECR 1280
Cdd:cd15648      1 VCQVCEKPGELLLCEGQCCGAFHLDCIGLSEMPSGKFICDECI 43

PHD4_NSD1

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1402-1441

1.15e-22

Pssm-ID: 277126 Cd Length: 40 Bit Score: 92.39 E-value: 1.15e-22

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDC 1441
Cdd:cd15656      1 WCFVCSEGGSLLCCESCPAAFHRECLNIDMPEGSWYCNDC 40

C5HCH

pfam17982

NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family ...

1854-1903

9.88e-20

Pssm-ID: 465605 Cd Length: 50 Bit Score: 84.44 E-value: 9.88e-20

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1854 WHQCDVCGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGP 1903
Cdd:pfam17982    1 WHQCSVCGSPATSFCEFCPSSFCKDHEKGALVPSALEGRLCCSEHDPESP 50

PWWP

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...

19-106

3.58e-14

Pssm-ID: 459964 [Multi-domain] Cd Length: 92 Bit Score: 70.15 E-value: 3.58e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   19 GDLIWAKFKRRPWWPCRICSDPLINTHSKMKvanRRPYREYYVEAFGDpSEKAWVAGKAIVMFEGRHQFEELpvLRKRGK 98
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVLKP---KKKDGEYLVRFFGD-SEFAWVKPKDLKPFDEGDEFEYL--KKKKKK 74


                   ....*...
gi 1958702498   99 QKEKGYRH 106
Cdd:pfam00855   75 KKKKAFKK 82

AWS

pfam17907

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...

1594-1632

3.44e-13

Pssm-ID: 465559 Cd Length: 39 Bit Score: 65.52 E-value: 3.44e-13

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1594 DENPCGIDSECINRMLLYECHPTVCPAGGRCQNQCFSKR 1632
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39

AWS

smart00570

associated with SET domains; subdomain of PRESET

1584-1634

4.06e-11

associated with SET domains; subdomain of PRESET

Pssm-ID: 197795 Cd Length: 50 Bit Score: 60.11 E-value: 4.06e-11

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958702498  1584 EIPRCNCKAT--DENPCGidSECINRMLLYEChPTVCPAGGRCQNQCFSKRQY 1634
Cdd:smart00570    1 DIMTCECKPTddDETACG--SDCLNRMLFIEC-SSSCPCGSYCSNQRFQKRQY 50

PHA03247

large tegument protein UL36; Provisional

1916-2288

4.34e-09

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 62.65 E-value: 4.34e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1916 PPTATLSPSPGtqqteqssemgtqgPKKSDQPPTDATQMlslSKKAVTGTCQRPllpERPPERTDSSShlldrirdlagS 1995
Cdd:PHA03247  2553 PPLPPAAPPAA--------------PDRSVPPPRPAPRP---SEPAVTSRARRP---DAPPQSARPRA-----------P 2601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1996 GTKSQSLVSSQRPQDRPPAKEGPRPQPPDRASPVTRPSSSPSVSSLPLERPLRMTEP---RLDKSIGAASPKSQAVEKPP 2072
Cdd:PHA03247  2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQ 2681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2073 APTglRLSSPDRLLN-TNSPKPQISDRPPDKSHASLTQRLPPPEKVLSAVVQSLVAkekalrPVDQNTQAKHRAAVVmDL 2151
Cdd:PHA03247  2682 RPR--RRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAL------PAAPAPPAVPAGPAT-PG 2752

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2152 IDLTPRQKERAASPQEVTAQADEKTPVLESSSRPT----SRGLGHVPRAVEKGGVSDPLQPPGKSAAPSEHPWQAVKSLT 2227
Cdd:PHA03247  2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT 2832

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 2228 HARFLSPPSAKAFLYESAIQASGRAPVGSEQTPGPPSPAPGLLK-----QVKQLSRGLTAKSGQSF 2288
Cdd:PHA03247  2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAaparpPVRRLARPAVSRSTESF 2898

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1402-1441

1.15e-08

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: 52.98 E-value: 1.15e-08

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1958702498  1402 WCFVCSE---GGSLLCCDSCPAAFHRECLNI----DIPEGNWYCNDC 1441
Cdd:smart00249    1 YCSVCGKpddGGELLQCDGCDRWYHQTCLGPplleEEPDGKWYCPKC 47

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1402-1442

2.42e-08

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: 52.11 E-value: 2.42e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958702498 1402 WCFVCS---EGGSLLCCDSCPAAFHRECLNI-----DIPEGNWYCNDCK 1442
Cdd:pfam00628    1 YCAVCGksdDGGELVQCDGCDDWFHLACLGPpldpaEIPSGEWLCPECK 49

PWWP

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

16-73

1.79e-07

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

Pssm-ID: 214603 [Multi-domain] Cd Length: 63 Bit Score: 50.04 E-value: 1.79e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958702498    16 YEVGDLIWAKFKRRPWWPCRICSDPLINTHskmKVANRRPYREYYVEAFGDPsEKAWV 73
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPKMTPDN---IMKRKSDENLYPVLFFGDK-DTAWI 54

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1238-1279

5.99e-06

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 45.28 E-value: 5.99e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1958702498  1238 VCQNCEKLGELLLCEaQCCGAFHLECLGLT---EMPRGKFICNEC 1279
Cdd:smart00249    4 VCGKPDDGGELLQCD-GCDRWYHQTCLGPPlleEEPDGKWYCPKC 47

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1238-1280

3.60e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 43.25 E-value: 3.60e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1238 VCQNCEKLGELLLCEaQCCGAFHLECLGLT----EMPRGKFICNECR 1280
Cdd:pfam00628    4 VCGKSDDGGELVQCD-GCDDWFHLACLGPPldpaEIPSGEWLCPECK 49

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1814-1855

5.74e-05

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 42.58 E-value: 5.74e-05

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1958702498  1814 CFSCG---DGGQLVSCKkpGCPKVYHADCLNLTKR---PAGKWECPWH 1855
Cdd:smart00249    2 CSVCGkpdDGGELLQCD--GCDRWYHQTCLGPPLLeeePDGKWYCPKC 47

Atrophin-1

pfam03154

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...

1922-2265

2.36e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 46.68 E-value: 2.36e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1922 SPS-PGTQQTEQSSEMGTQGPKKSDQPPTDATQ--MLSLSKKAVTGTCQR------PLLPERPPERTDSSSHLLDRIRDL 1992
Cdd:pfam03154  145 SPSiPSPQDNESDSDSSAQQQILQTQPPVLQAQsgAASPPSPPPPGTTQAatagptPSAPSVPPQGSPATSQPPNQTQST 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1993 AGSGTKSQSLVS--SQR-PQDRPPAKEGPRPQPPDRASPVTRPSSSPSVSSLPLERPLR-----MTEPRLDKSIGAASPK 2064
Cdd:pfam03154  225 AAPHTLIQQTPTlhPQRlPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQtgpshMQHPVPPQPFPLTPQS 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2065 SQAvEKPPAPTGlrlsspdrllNTNSPKPQISDRPPDKSHASLTQrlPPPEKVLSAVVQSLV-AKEKALRPVDQ--NTQA 2141
Cdd:pfam03154  305 SQS-QVPPGPSP----------AAPGQSQQRIHTPPSQSQLQSQQ--PPREQPLPPAPLSMPhIKPPPTTPIPQlpNPQS 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2142 -KHRAAVvmdlidltprqkeRAASPQEVTAQADEKTPVLESSSRPTSRGLGHVPRAVEKGGVSDPLQPPgksaaPSEHPw 2220
Cdd:pfam03154  372 hKHPPHL-------------SGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPP-----PAQPP- 432

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 2221 qavkSLTHARFLSPPSAkaflyeSAIQASGRAPVGSeQTPGPPSP 2265
Cdd:pfam03154  433 ----VLTQSQSLPPPAA------SHPPTSGLHQVPS-QSPFPQHP 466

TNG2

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

1147-1280

1.33e-03

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

Pssm-ID: 227367 [Multi-domain] Cd Length: 271 Bit Score: 43.00 E-value: 1.33e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1147 KEFGGGTTRIFDKPRKRKRqrhGTARVHYKRVKKEDSARETPSSAEGELmIHRTAASPKEILEEGIEHDPGMSASKRLQG 1226
Cdd:COG5034    144 EHRSAASSQGSRHTKLKKR---KNIHNLKRRSPELSSKREVSFTLESPS-VPDTATRVKEGNNGGSTKSRGVSSEDNSEG 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 1227 ERgggaalKENVCQNCEkLGELLLCEAQCCGA--FHLECLGLTEMPRGKFICNECR 1280
Cdd:COG5034    220 EE------LYCFCQQVS-YGQMVACDNANCKRewFHLECVGLKEPPKGKWYCPECK 268

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1814-1860

3.90e-03

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 37.47 E-value: 3.90e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958702498 1814 CFSCGDGGQLVSCKkpGCPKVYHADCLNLTKRPA----GKWECPwhQCDVC 1860
Cdd:pfam00628    5 CGKSDDGGELVQCD--GCDDWFHLACLGPPLDPAeipsGEWLCP--ECKPK 51

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1285-1331

3.91e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 37.19 E-value: 3.91e-03

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1958702498  1285 TCFVCKQSGEDVK--RCLLplCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:smart00249    1 YCSVCGKPDDGGEllQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

TNG2

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

1402-1442

7.11e-03

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

Pssm-ID: 227367 [Multi-domain] Cd Length: 271 Bit Score: 40.69 E-value: 7.11e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1402 WCFvCSEG--GSLLCCDS--CPAA-FHRECLNI-DIPEGNWYCNDCK 1442
Cdd:COG5034    223 YCF-CQQVsyGQMVACDNanCKREwFHLECVGLkEPPKGKWYCPECK 268

TNG2

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

1778-1853

9.12e-03

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

Pssm-ID: 227367 [Multi-domain] Cd Length: 271 Bit Score: 40.31 E-value: 9.12e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1778 PKNQPIVTEeksrkFKRKPHGKRRSQGEVTKEREDE--CFsCGDG--GQLVSCKKPGCPKV-YHADCLNLTKRPAGKWEC 1852
Cdd:COG5034    191 PDTATRVKE-----GNNGGSTKSRGVSSEDNSEGEElyCF-CQQVsyGQMVACDNANCKREwFHLECVGLKEPPKGKWYC 264


                   .
gi 1958702498 1853 P 1853
Cdd:COG5034    265 P 265

Name

Accession

Description

Interval

E-value

SET_NSD1

cd19210

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...

1634-1775

2.12e-106

Pssm-ID: 380987 [Multi-domain] Cd Length: 142 Bit Score: 335.74 E-value: 2.12e-106

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1634 YPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 1713
Cdd:cd19210      1 YPEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498 1714 HCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1775
Cdd:cd19210     81 HCCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 142

SET_NSD

cd19173

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...

1634-1775

1.55e-102

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: 324.65 E-value: 1.55e-102

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1634 YPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 1713
Cdd:cd19173      1 YPPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNITNFYMLTLDKDRIIDAGPKGNLSRFMN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498 1714 HCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1775
Cdd:cd19173     81 HSCQPNCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNEKKVCRCGAPNCSGFLG 142

SET_NSD2

cd19211

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...

1634-1775

4.63e-94

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: 300.37 E-value: 4.63e-94

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1634 YPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 1713
Cdd:cd19211      1 YPETKIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498 1714 HCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1775
Cdd:cd19211     81 HSCQPNCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGAPNCSGFLG 142

SET_NSD3

cd19212

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...

1634-1775

2.46e-89

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: 286.82 E-value: 2.46e-89

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1634 YPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 1713
Cdd:cd19212      1 YPDAEIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498 1714 HCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1775
Cdd:cd19212     81 HSCNPNCETQKWTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTECHCGADNCSGFLG 142

SET_SETD2-like

cd10531

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...

1636-1771

1.49e-72

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: 238.69 E-value: 1.49e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1636 DVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHC 1715
Cdd:cd10531      1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFINHS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 1716 CQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCS 1771
Cdd:cd10531     81 CEPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNYNEAKQVCLCGAQNCR 136

PWWP_NSD1_rpt1

cd20161

first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...

13-128

2.65e-71

Pssm-ID: 438989 Cd Length: 116 Bit Score: 234.29 E-value: 2.65e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   13 PLKYEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVANRRPYREYYVEAFGDPSEKAWVAGKAIVMFEGRHQFEELPV 92
Cdd:cd20161      1 PVKYEVGDLVWAKFSRRPWWPCRICADPLLDTHSKMKVPSRRPCRQYYVETLGELTEKAWVAAKAVVPFEGRHQFEELPV 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958702498   93 LRKRGKQKEKGYRHKVPQKILSKWEASVGLAEQCDV 128
Cdd:cd20161     81 LRRRGKQKEKDYKHKIPQKLLSLWEASVAHAEDFLS 116

PWWP_NSD1_rpt2

cd20164

second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...

1448-1543

3.77e-69

Pssm-ID: 438992 Cd Length: 96 Bit Score: 227.07 E-value: 3.77e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1448 HYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 1527
Cdd:cd20164      1 HYKEVVWVKVGRYRWWPAEVCHPKSIPTNIQKMKHDIGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 80

                           90
                   ....*....|....*.
gi 1958702498 1528 KKALQEAAARFEELKA 1543
Cdd:cd20164     81 KKALQEAAVRFEELKA 96

SET_SETD2

cd19172

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...

1634-1775

4.53e-66

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: 220.15 E-value: 4.53e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1634 YPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 1713
Cdd:cd19172      1 YAKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFMALKSDEIIDATKKGNLSRFIN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498 1714 HCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1775
Cdd:cd19172     81 HSCEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFERYGKEAQKCYCGSPNCRGYIG 142

SET_ASH1L

cd19174

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...

1636-1775

6.07e-58

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: 196.74 E-value: 6.07e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1636 DVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRyAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHC 1715
Cdd:cd19174      1 GLERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMI-EQYHNHSHHYCLNLDSGMVIDGYRMGNEARFVNHS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958702498 1716 CQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLG-NGKTVCKCGAPNCSGFLG 1775
Cdd:cd19174     80 CDPNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNvEKQQPCKCGSPNCRGVIG 140

SET_ASHR3-like

cd19175

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...

1637-1775

7.50e-56

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: 190.71 E-value: 7.50e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1637 VEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCC 1716
Cdd:cd19175      2 MKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGEKNFYMCEIDKDMVIDATFKGNLSRFINHSC 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958702498 1717 QPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNgKTVCKCGAPNCSGFLG 1775
Cdd:cd19175     82 DPNCELQKWQVDGETRIGVFAIRDIKKGEELTYDYQFVQFGA-DQDCHCGSKNCRGKLG 139

PWWP_NSD_rpt2

cd05838

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1448-1543

2.25e-52

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: 178.97 E-value: 2.25e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1448 HYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 1527
Cdd:cd05838      1 LYGDIVWVKLGNYRWWPAEILHPREVPDNIQSLPHPPGEFPVRFFGSHDYYWVHRGRVFLFEEGDKGSKEKSKKSLDKSF 80

                           90
                   ....*....|....*.
gi 1958702498 1528 KKALQEAAARFEELKA 1543
Cdd:cd05838     81 KRALKEANEAFRELKA 96

PWWP_NSD2_rpt2

cd20165

second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar ...

1448-1542

3.91e-50

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: 172.83 E-value: 3.91e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1448 HYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 1527
Cdd:cd20165      1 RFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSKYQGGKGIGKVF 80

                           90
                   ....*....|....*
gi 1958702498 1528 KKALQEAAARFEELK 1542
Cdd:cd20165     81 KNALQEAEARFREIK 95

PWWP_NSD3_rpt2

cd20166

second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar ...

1448-1543

5.82e-48

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: 166.69 E-value: 5.82e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1448 HYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGvDGTY 1527
Cdd:cd20166      1 HYKQIVWVKLGNYRWWPAEICNPRSVPLNIQGLKHDIGDFPVFFFGSHDYYWVHQGRVFPYVEGDKSFAEGQTSI-NKTF 79

                           90
                   ....*....|....*.
gi 1958702498 1528 KKALQEAAARFEELKA 1543
Cdd:cd20166     80 KKALEEAAKRFQELKA 95

SET

smart00317

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

1635-1758

2.79e-47

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: 165.59 E-value: 2.79e-47

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498  1635 PDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNH 1714
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1958702498  1715 CCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGN 1758
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

SET_SETD1-like

cd10518

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...

1646-1770

4.19e-40

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: 146.20 E-value: 4.19e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKW 1725
Cdd:cd10518     25 GWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGGGTYMFRIDEDLVIDATKKGNIARFINHSCDPNCYAKII 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1726 SVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNC 1770
Cdd:cd10518    105 TVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEEKIPCLCGAPNC 149

PWWP_NSD_rpt1

cd20144

first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

18-125

1.10e-37

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: 137.83 E-value: 1.10e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   18 VGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVANRRPYREYYVEAFGDPSEKAWVAGKAIVMFEGRHQFEELPVLRKRG 97
Cdd:cd20144      1 VGDLVWAKVSGHPWWPCMVTYDPESGLYTKIKGSGGRTYRQYHVQFFGDNGERGWVSEKSLMPFEGKEKFEELVKELKKK 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958702498   98 ----KQKEKgYRHKVPQKILSKWEASVGLAEQ 125
Cdd:cd20144     81 akkkSKKAK-LEKKVKPSRRKKWEIAVEEAEE 111

SET_SUV39H

cd10542

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

1611-1774

1.28e-35

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: 137.04 E-value: 1.28e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1611 YECHPTvCPAGGRCQNQCFSK-RQYPdVEIFRT-LQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITn 1688
Cdd:cd10542     64 YECNSR-CKCGPDCPNRVVQRgRKVP-LCIFRTsNGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGRT- 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1689 fYMLTLDKDRI-----IDAGPKGNYARFMNHCCQPNCET-QKWSVNGDT---RVGLFALSDIKAGTELTFNYNL------ 1753
Cdd:cd10542    141 -YLFDLDYNDDdceytVDAAYYGNISHFINHSCDPNLAVyAVWINHLDPrlpRIAFFAKRDIKAGEELTFDYLMtgtggs 219

                          170       180
                   ....*....|....*....|....*.
gi 1958702498 1754 -ECLGNGK----TVCKCGAPNCSGFL 1774
Cdd:cd10542    220 sESTIPKPkdvrVPCLCGSKNCRKYL 245

SET_EZH

cd10519

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...

1646-1751

9.18e-33

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: 123.89 E-value: 9.18e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGELIDEEEcrARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKW 1725
Cdd:cd10519     12 GWGLFLKEPIKKDEFIGEYTGELISQDE--ADRRGKIYDKYNSSYLFNLNDQFVVDATRKGNKIRFANHSSNPNCYAKVM 89

                           90       100
                   ....*....|....*....|....*.
gi 1958702498 1726 SVNGDTRVGLFALSDIKAGTELTFNY 1751
Cdd:cd10519     90 MVNGDHRIGIFAKRDIEAGEELFFDY 115

SET_SETDB-like

cd10538

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...

1561-1752

1.30e-32

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: 127.10 E-value: 1.30e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1561 PPYKHIKVNRPIGRVQIFTADLSE-----IPRC---NCKATDENP--CGIDSECINRM-----LLYECHPTvCPAGGRCQ 1625
Cdd:cd10538      1 PSFTYIKDNIVGKNVQPFSNIIDSvgckcKDDCldsKCACAAESDgiFAYTKNGLLRLnnsppPIFECNSK-CSCDDDCK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1626 NQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITnfYMLTLDKDR------- 1698
Cdd:cd10538     80 NRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSGGS--YLFDLDEFSdsdgdge 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1699 --IIDAGPKGNYARFMNHCCQPNCETQK-WSVNGDT---RVGLFALSDIKAGTELTFNYN 1752
Cdd:cd10538    158 elCVDATFCGNVSRFINHSCDPNLFPFNvVIDHDDLrypRIALFATRDILPGEELTFDYG 217

SET

COG2940

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

1635-1772

1.86e-32

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 123.92 E-value: 1.86e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1635 PDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItnfYMLTLDKDRIIDAGPKGNYARFMNH 1714
Cdd:COG2940      6 PRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT---YLFELDDDGVIDGALGGNPARFINH 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958702498 1715 CCQPNCETqkwsVNGDTRVGLFALSDIKAGTELTFNYNLEClGNGKTVCKCgaPNCSG 1772
Cdd:COG2940     83 SCDPNCEA----DEEDGRIFIVALRDIAAGEELTYDYGLDY-DEEEYPCRC--PNCRG 133

SET_SETMAR

cd10544

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...

1585-1774

8.44e-32

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: 126.26 E-value: 8.44e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1585 IPRCNCKatdENPCGIDSE-CI---------NRMLL----------YECHpTVCPAGGRCQNQCFSKRQYPDVEIFRTLQ 1644
Cdd:cd10544     24 FPGCDCK---TSSCEPETCsCLrkygpnyddDGCLLdfdgkysgpvFECN-SMCKCSESCQNRVVQNGLQFKLQVFKTPK 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1645 RGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRyAQEHDITNfYMLTLDKDR--------IIDAGPKGNYARFMNHCC 1716
Cdd:cd10544    100 KGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTK-SQTKGDMN-YIIVLREHLssgkvletFVDPTYIGNIGRFLNHSC 177

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498 1717 QPNCETQKWSVNGDT-RVGLFALSDIKAGTELTFNY-----NLECLGN--------GKTVCKCGAPNCSGFL 1774
Cdd:cd10544    178 EPNLFMVPVRVDSMVpKLALFAARDIVAGEELSFDYsgefsNSVESVTlarqdeskSRKPCLCGAENCRGFL 249

PHD3_NSD1

cd15653

PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1332-1385

1.46e-31

Pssm-ID: 277123 Cd Length: 54 Bit Score: 118.10 E-value: 1.46e-31

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958702498 1332 ICITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSKILASNSIICPNH 1385
Cdd:cd15653      1 ICLTCHATNPSNPSASKGRLMRCVRCPVAYHANDFCLAAGSVILASNSIICPNH 54

SET_SETDB1

cd10517

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...

1610-1774

9.82e-31

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: 124.32 E-value: 9.82e-31

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1610 LYECHPTvCPAGGRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEEcrariryAQEH--DIT 1687
Cdd:cd10517    105 VYECNSR-CKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQILTEDE-------ANEEglQYG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1688 NFYMLTLD--------KDR----------IIDAGPKGNYARFMNHCCQPNCETQKWSVNG-DTR---VGLFALSDIKAGT 1745
Cdd:cd10517    177 DEYFAELDyievveklKEGyesdveehcyIIDAKSEGNLGRYLNHSCSPNLFVQNVFVDThDLRfpwVAFFASRYIRAGT 256

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958702498 1746 ELTFNYNLEcLGN--GKTV-CKCGAPNCSGFL 1774
Cdd:cd10517    257 ELTWDYNYE-VGSvpGKVLyCYCGSSNCRGRL 287

SET

pfam00856

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...

1646-1752

2.26e-30

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 117.24 E-value: 2.26e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGE-LIDEEECRARIRYAQEHDIT---NFYMLTLDKD--RIID--AGPKGNYARFMNHCCQ 1717
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELrlwGPYLFTLDEDseYCIDarALYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958702498 1718 PNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYN 1752
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

SET_SUV39H_DIM5-like

cd19473

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...

1607-1774

3.12e-30

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: 122.43 E-value: 3.12e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1607 RMLLYECHPTvCPAGGRCQNQCFSK-RQYPdVEIFRT-LQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRAR---IRYA 1681
Cdd:cd19473     78 RLPIYECHEG-CACSDDCPNRVVERgRKVP-LQIFRTsDGRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRrdaATIA 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1682 QEHDItnfYMLTLDK--------DRI------ID----AGPkgnyARFMNHCCQPNCETqkWSVNGDT------RVGLFA 1737
Cdd:cd19473    156 QRKDV---YLFALDKfsdpdsldPRLrgdpyeIDgefmSGP----TRFINHSCDPNLRI--FARVGDHadkhihDLAFFA 226

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1738 LSDIKAGTELTFNY-----------NLECLGNGKTVCKCGAPNCSGFL 1774
Cdd:cd19473    227 IKDIPRGTELTFDYvdgvtgldddaGDEEKEKEMTKCLCGSPKCRGYL 274

SET_KMT2A_2B

cd19170

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...

1637-1774

9.35e-29

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: 114.03 E-value: 9.35e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1637 VEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItNFYMLTLDKDRIIDAGPKGNYARFMNHCC 1716
Cdd:cd19170     16 VGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGI-GCYMFRIDDDEVVDATMHGNAARFINHSC 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958702498 1717 QPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLEcLGNGKTVCKCGAPNCSGFL 1774
Cdd:cd19170     95 EPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFP-IEDVKIPCTCGSKKCRKYL 151

SET_SET1

cd20072

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...

1647-1770

2.50e-28

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: 112.52 E-value: 2.50e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1647 WGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWS 1726
Cdd:cd20072     25 WGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGSSYLFRIDDDTVVDATKKGNIARFINHCCDPNCTAKIIK 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1727 VNGDTRVGLFALSDIKAGTELTFNYNLECLGNgKTVCKCGAPNC 1770
Cdd:cd20072    105 VEGEKRIVIYAKRDIAAGEELTYDYKFPREED-KIPCLCGAPNC 147

PWWP

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...

1451-1539

2.52e-28

Pssm-ID: 459964 [Multi-domain] Cd Length: 92 Bit Score: 110.21 E-value: 2.52e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDV--SSKDKMGKGVDGTYK 1528
Cdd:pfam00855    2 DLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEfeYLKKKKKKKKKKAFK 81

                           90
                   ....*....|.
gi 1958702498 1529 KALQEAAARFE 1539
Cdd:pfam00855   82 KALEEAEEALK 92

SET_SUV39H2

cd10532

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

1610-1774

5.44e-28

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: 114.99 E-value: 5.44e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1610 LYECHpTVCPAGGRCQNQCFSKRQYPDVEIFRTLQ-RGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITN 1688
Cdd:cd10532     60 IYECN-SRCKCGPDCPNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGITY 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1689 FYMLTLDKDRI-IDAGPKGNYARFMNHCCQPNceTQKWSV---NGDT---RVGLFALSDIKAGTELTFNYNLECLGN--- 1758
Cdd:cd10532    139 LFDLDYESDEFtVDAARYGNVSHFVNHSCDPN--LQVFNVfidNLDTrlpRIALFSTRTIKAGEELTFDYQMKGSGDlss 216

                          170       180
                   ....*....|....*....|....*..
gi 1958702498 1759 -----------GKTVCKCGAPNCSGFL 1774
Cdd:cd10532    217 dsidnspakkrVRTVCKCGAVTCRGYL 243

SET_KMT2C_2D

cd19171

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...

1641-1770

7.38e-28

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: 111.37 E-value: 7.38e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1641 RTLQRGWGLRTKTDIKKGEFVNEYVGELIDEE--ECRARIRYAQEHDItnfYMLTLDKDRIIDAGPKGNYARFMNHCCQP 1718
Cdd:cd19171     20 RSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEvaNRREKIYESQNRGI---YMFRIDNDWVIDATMTGGPARYINHSCNP 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958702498 1719 NCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNG-KTVCKCGAPNC 1770
Cdd:cd19171     97 NCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQhKIPCLCGAPNC 149

SET_SETD1

cd19169

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...

1646-1770

8.98e-28

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: 110.89 E-value: 8.98e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGELI-----DEEEcrarIRYAQEhDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNC 1720
Cdd:cd19169     24 DWGLFALEPIAADEMVIEYVGQVIrqsvaDERE----KRYEAI-GIGSSYLFRVDDDTIIDATKCGNLARFINHSCNPNC 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1721 ETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLEcLGNGKTVCKCGAPNC 1770
Cdd:cd19169     99 YAKIITVESQKKIVIYSKRPIAVNEEITYDYKFP-IEDEKIPCLCGAPQC 147

SET_LegAS4-like

cd10522

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...

1646-1752

1.82e-27

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: 108.97 E-value: 1.82e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEhditNFYMLTLDKD-RIIDAGPKGNYARFMNHCCQPNCETQK 1724
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYD----PLYPFDLNGDiLVIDAGKKGNLTRFINHSDQPNLELIV 89

                           90       100
                   ....*....|....*....|....*...
gi 1958702498 1725 WSVNGDTRVGLFALSDIKAGTELTFNYN 1752
Cdd:cd10522     90 RTLKGEQHIGFVAIRDIKPGEELFISYG 117

PHD5_NSD1

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1813-1855

9.31e-27

Pssm-ID: 277129 Cd Length: 43 Bit Score: 104.25 E-value: 9.31e-27

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1813 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 1855
Cdd:cd15659      1 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 43

PHD2_NSD1

cd15650

PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1285-1331

5.44e-26

Pssm-ID: 277120 Cd Length: 47 Bit Score: 102.27 E-value: 5.44e-26

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1285 TCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:cd15650      1 TCFVCKKSDEDVRRCMLPLCGKFYHEECVLKYPPTVMQNRGFRCSLH 47

PWWP_NSD2_rpt1

cd20162

first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...

16-125

1.03e-25

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: 104.22 E-value: 1.03e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   16 YEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKvANRRPYREYYVEAFGDPSEKAWVAGKAIVMFEGRHQFEEL---PV 92
Cdd:cd20162      1 YNVGDLVWSKVSGYPWWPCMVSADPLLHSHTKLK-GQKKSARQYHVQFFGDAPERAWIFEKSLVPFEGEGQFEQLcqeSA 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958702498   93 LRKRGKQKEKGYRHKVPQKILSKWEASVGLAEQ 125
Cdd:cd20162     80 KQAPTKAEKIKLLKPISGKLRAQWDMGIVQAEE 112

PWWP

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

1447-1509

1.53e-25

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

Pssm-ID: 214603 [Multi-domain] Cd Length: 63 Bit Score: 101.27 E-value: 1.53e-25

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958702498  1447 PHYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYM 1509
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63

SET_EHMT

cd10543

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

1565-1770

2.02e-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: 107.04 E-value: 2.02e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1565 HIKVNRPIGRVQIFTA-DLSEIPRCNCKATDENpCGIDSEC--------INRMLLYECHPtVCPAGGRCQNQCFSKRQYP 1635
Cdd:cd10543     14 PLNIDRNITSLQTCSCrDDCSSDNCVCGRLSVR-CWYDKEGrllpdfnkLDPPLIFECNR-ACSCWRNCRNRVVQNGIRY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1636 DVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDItnfYMLTLD-KDR---IIDAGPKGNYARF 1711
Cdd:cd10543     92 RLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSR-----EDDS---YLFDLDnKDGetyCIDARRYGNISRF 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1712 MNHCCQPNCETQKWSVNGDT----RVGLFALSDIKAGTELTFNYnleclGN------GKTV-CKCGAPNC 1770
Cdd:cd10543    164 INHLCEPNLIPVRVFVEHQDlrfpRIAFFASRDIKAGEELGFDY-----GEkfwrikGKYFtCRCGSPKC 228

PWWP_NSD3_rpt1

cd20163

first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...

16-125

1.69e-24

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: 100.78 E-value: 1.69e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   16 YEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMkvaNRRPYREYYVEAFGDPSEKAWVAGKAIVMFEGRHQFEEL--PVL 93
Cdd:cd20163      1 FQVGDLVWSKVGTYPWWPCMVSSDPQLEVHTKI---NTRGAREYHVQFFSSQPERAWVHEKRVREYKGHKQYEELlaEAT 77

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958702498   94 RKRGKQKEK-GYRHKVPQKILSKWEASVGLAEQ 125
Cdd:cd20163     78 KQASNHSEKqKIRKPRPQRERAQWDIGIAHAEK 110

SET_AtSUVH-like

cd10545

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...

1609-1752

7.90e-24

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: 102.48 E-value: 7.90e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1609 LLYECHPTvCPAGGRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEEcrARIRYAQEH---D 1685
Cdd:cd10545     61 AIYECGPL-CKCPPSCYNRVTQKGLRYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSE--ADTRSGNDDylfD 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1686 ITNFY----------MLTLDKDR-------------IIDAGPKGNYARFMNHCCQPNCETQKWSV-NGDTR---VGLFAL 1738
Cdd:cd10545    138 IDNRQtnrgwdggqrLDVGMSDGerssaedeessefTIDAGSFGNVARFINHSCSPNLFVQCVLYdHNDLRlprVMLFAA 217

                          170
                   ....*....|....
gi 1958702498 1739 SDIKAGTELTFNYN 1752
Cdd:cd10545    218 DNIPPLQELTYDYG 231

PHD3_NSD2

cd15654

PHD finger 3 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1333-1385

9.16e-24

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: 96.07 E-value: 9.16e-24

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958702498 1333 CITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSKILASNSIICPNH 1385
Cdd:cd15654      2 CVSCHASNPSNPRATKGKMMRCVRCPVAYHGGDLCIAAGCAVLTSNSIICTNH 54

SET_SUV39H1

cd10525

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

1610-1774

5.19e-23

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: 100.74 E-value: 5.19e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1610 LYECHpTVCPAGGRCQNQCFSKRQYPDVEIFRTLQ-RGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITN 1688
Cdd:cd10525     62 IYECN-SRCRCGPDCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATY 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1689 FYMLTLDKD-RIIDAGPKGNYARFMNHCCQPNceTQKWSVNGDT------RVGLFALSDIKAGTELTFNYNLEC------ 1755
Cdd:cd10525    141 LFDLDYVEDvYTVDAAYYGNISHFVNHSCDPN--LQVYNVFIDNlderlpRIALFATRTIRAGEELTFDYNMQVdpvdae 218

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958702498 1756 -------LGNG----------KTVCKCGAPNCSGFL 1774
Cdd:cd10525    219 stkmdsnFGLAglpgspkkrvRIECKCGVRSCRKYL 254

PHD5_NSD

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1813-1855

9.42e-23

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: 92.78 E-value: 9.42e-23

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1813 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 1855
Cdd:cd15568      1 ECFRCGDGGDLVLCDFKGCPKVYHLSCLGLEKPPGGKWICPWH 43

PHD1_NSD1_2

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...

1238-1280

1.14e-22

Pssm-ID: 277118 Cd Length: 43 Bit Score: 92.54 E-value: 1.14e-22

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1238 VCQNCEKLGELLLCEAQCCGAFHLECLGLTEMPRGKFICNECR 1280
Cdd:cd15648      1 VCQVCEKPGELLLCEGQCCGAFHLDCIGLSEMPSGKFICDECI 43

PHD4_NSD1

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1402-1441

1.15e-22

Pssm-ID: 277126 Cd Length: 40 Bit Score: 92.39 E-value: 1.15e-22

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDC 1441
Cdd:cd15656      1 WCFVCSEGGSLLCCESCPAAFHRECLNIDMPEGSWYCNDC 40

SET_KMT2A

cd19206

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...

1637-1774

1.92e-22

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: 95.86 E-value: 1.92e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1637 VEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItNFYMLTLDKDRIIDAGPKGNYARFMNHCC 1716
Cdd:cd19206     16 VGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGI-GCYMFRIDDSEVVDATMHGNAARFINHSC 94

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1717 QPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYN--LECLGNgKTVCKCGAPNCSGFL 1774
Cdd:cd19206     95 EPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKfpIEDASN-KLPCNCGAKKCRKFL 153

SET_EZH2

cd19218

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...

1646-1751

2.07e-22

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: 94.59 E-value: 2.07e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITnfYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKW 1725
Cdd:cd19218     15 GWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCS--FLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVM 92

                           90       100
                   ....*....|....*....|....*.
gi 1958702498 1726 SVNGDTRVGLFALSDIKAGTELTFNY 1751
Cdd:cd19218     93 MVNGDHRIGIFAKRAIQTGEELFFDY 118

SET_EHMT1

cd10535

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

1609-1770

1.22e-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: 96.16 E-value: 1.22e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1609 LLYECHpTVCPAGGRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDItn 1688
Cdd:cd10535     66 LIFECN-HACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-----EEDS-- 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1689 fYMLTLD-KDR---IIDAGPKGNYARFMNHCCQPN-CETQKWSVNGD---TRVGLFALSDIKAGTELTFNYNLECLG-NG 1759
Cdd:cd10535    138 -YLFDLDnKDGevyCIDARFYGNVSRFINHHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDiKG 216

                          170
                   ....*....|..
gi 1958702498 1760 KTV-CKCGAPNC 1770
Cdd:cd10535    217 KLFsCRCGSPKC 228

SET_EZH1

cd19217

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...

1646-1751

1.55e-21

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: 92.82 E-value: 1.55e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHdiTNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKW 1725
Cdd:cd19217     17 GWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKY--MSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVV 94

                           90       100
                   ....*....|....*....|....*.
gi 1958702498 1726 SVNGDTRVGLFALSDIKAGTELTFNY 1751
Cdd:cd19217     95 MVNGDHRIGIFAKRAIQQGEELFFDY 120

SET_SUV39H_Clr4-like

cd20073

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...

1581-1774

1.74e-21

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: 96.49 E-value: 1.74e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1581 DLSEIPRCNC-KATDENPCGIDSE----CINRMLLYECHPTvCPAGGRCQNQCFSK-RQYPdVEIFRTLQRGWGLRTKTD 1654
Cdd:cd20073     35 DLNNPGSCQClEDSNEKSFAYDEYgrvrANTGSIIYECNEN-CDCGINCPNRVVQRgRKLP-LEIFKTKHKGWGLRCPRF 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1655 IKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRI-----IDAGPKGNYARFMNHCCQPNCETQKWSVNG 1729
Cdd:cd20073    113 IKAGTFIGVYLGEVITQSEAEIRGKKYDNVGVTYLFDLDLFEDQVdeyytVDAQYCGDVTRFINHSCDPNLAIYSVLRDK 192

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 1730 DTR----VGLFALSDIKAGTELTFNYN-------LECLGNGKTV----------CKCGAPNCSGFL 1774
Cdd:cd20073    193 SDSkiydLAFFAIKDIPALEELTFDYSgrnnfdqLGFIGNRSNSkyinlknkrpCYCGSANCRGWL 258

SET_SETD1A

cd19204

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...

1647-1774

1.02e-20

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: 90.85 E-value: 1.02e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1647 WGLRTKTDIKKGEFVNEYVGELIDEEECRAR-IRYAQEhDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKW 1725
Cdd:cd19204     26 WGLFAMEPIAADEMVIEYVGQNIRQVVADMReKRYVQE-GIGSSYLFRVDHDTIIDATKCGNLARFINHCCTPNCYAKVI 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958702498 1726 SVNGDTRVGLFALSDIKAGTELTFNYNLEcLGNGKTVCKCGAPNCSGFL 1774
Cdd:cd19204    105 TIESQKKIVIYSKQPIGVNEEITYDYKFP-IEDNKIPCLCGTENCRGTL 152

SET_EZH-like

cd19168

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...

1640-1751

1.25e-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: 89.56 E-value: 1.25e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1640 FRTLQRGWGLRTKTDIKKGEFVNEYVGELI-DEEECRARIRYAqehDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQP 1718
Cdd:cd19168      7 KSQLECGLGLFAAEDIKEGEFVIEYTGELIsHDEGVRREHRRG---DVSYLYLFEEQEGIWVDAAIYGNLSRYINHATDK 83

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958702498 1719 ----NCETQKWSVNGDTRVGLFALSDIKAGTELTFNY 1751
Cdd:cd19168     84 vktgNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120

SET_SETDB

cd10541

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...

1610-1774

3.06e-20

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: 92.22 E-value: 3.06e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1610 LYECHPTVCPAGGRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEecrarirYAQEHDIT-- 1687
Cdd:cd10541     67 VYECNKLCKCDPNMCQNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDD-------FADKEGLEmg 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1688 NFYMLTLDKDR----IIDAGPKGNYARFMNHCCQPNCETQKWSVNGDTR----VGLFALSDIKAGTELTFNYNLEC--LG 1757
Cdd:cd10541    140 DEYFANLDHIEescyIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLrfpwVAFFASKRIKAGTELTWDYNYEVgsVE 219

                          170
                   ....*....|....*..
gi 1958702498 1758 NGKTVCKCGAPNCSGFL 1774
Cdd:cd10541    220 GKELLCCCGSNECRGRL 236

PHD4_NSD

cd15567

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1402-1441

3.39e-20

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: 85.38 E-value: 3.39e-20

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNID-IPEGNWYCNDC 1441
Cdd:cd15567      1 WCFICSEGGSLICCESCPASFHPECLGLEpPPEGKFYCEDC 41

C5HCH

pfam17982

NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family ...

1854-1903

9.88e-20

Pssm-ID: 465605 Cd Length: 50 Bit Score: 84.44 E-value: 9.88e-20

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1854 WHQCDVCGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGP 1903
Cdd:pfam17982    1 WHQCSVCGSPATSFCEFCPSSFCKDHEKGALVPSALEGRLCCSEHDPESP 50

SET_SETDB2

cd10523

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...

1610-1774

1.54e-19

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: 91.05 E-value: 1.54e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1610 LYECHPTVCPAGGRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIdeeeCRAR---------IRY 1680
Cdd:cd10523     83 LYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVL----SRARspteplppkLEL 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1681 AQEHDI-TNFYMLTLDKDR-------IIDAGPKGNYARFMNHCCQPNCETQKWSVNGDTR----VGLFALSDIKAGTELT 1748
Cdd:cd10523    159 PSENEVeVVTSWLILSKKRklrenvcFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELT 238

                          170       180
                   ....*....|....*....|....*...
gi 1958702498 1749 FNYNLE--CLGNGKTVCKCGAPNCSGFL 1774
Cdd:cd10523    239 WDYSYDagTSPEQEIPCLCGVNKCQKKI 266

SET_SETD1B

cd19205

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...

1647-1774

3.12e-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: 86.65 E-value: 3.12e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1647 WGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWS 1726
Cdd:cd19205     26 WGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFARFINHSCNPNCYAKVIT 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1727 VNGDTRVGLFALSDIKAGTELTFNYNLEcLGNGKTVCKCGAPNCSGFL 1774
Cdd:cd19205    106 VESQKKIVIYSKQHINVNEEITYDYKFP-IEDVKIPCLCGSENCRGTL 152

SET_EHMT2

cd10533

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

1609-1770

4.92e-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: 4.92e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1609 LLYECHpTVCPAGGRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARiryaqEHDItn 1688
Cdd:cd10533     66 LIFECN-QACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-----EDDS-- 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1689 fYMLTLD-KD---RIIDAGPKGNYARFMNHCCQPN-CETQKWSVNGD---TRVGLFALSDIKAGTELTFNYN--LECLGN 1758
Cdd:cd10533    138 -YLFDLDnKDgevYCIDARYYGNISRFINHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYGdrFWDIKS 216

                          170
                   ....*....|..
gi 1958702498 1759 GKTVCKCGAPNC 1770
Cdd:cd10533    217 KYFTCQCGSEKC 228

PHD4_NSD3

cd15658

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1402-1441

7.22e-19

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: 81.50 E-value: 7.22e-19

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDC 1441
Cdd:cd15658      1 FCFVCARGGRLLCCESCPASFHPECLSIEMPEGCWNCNEC 40

SET_SETD8

cd10528

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...

1646-1751

1.42e-18

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: 84.17 E-value: 1.42e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1646 GWGLRTKTDIKKGEFVNEYVGELIDEEECRAR-IRYAQEHDItNFYML---TLDKDRIIDA-GPKGNYARFMNH-CCQPN 1719
Cdd:cd10528     28 GRGVIATRPFEKGDFVVEYHGDLITITEAKKReALYAKDPST-GCYMYyfqYKGKTYCVDAtKESGRLGRLINHsKKKPN 106

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958702498 1720 CETQKWSVNGDTRVGLFALSDIKAGTELTFNY 1751
Cdd:cd10528    107 LKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138

PHD5_NSD2

cd15660

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1813-1855

5.14e-18

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: 79.21 E-value: 5.14e-18

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1813 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 1855
Cdd:cd15660      1 ECFRCGDGGQLVLCDRKSCTKAYHLSCLGLTKRPFGKWECPWH 43

SET_KMT2B

cd19207

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...

1637-1774

6.36e-18

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: 82.76 E-value: 6.36e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1637 VEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItNFYMLTLDKDRIIDAGPKGNYARFMNHCC 1716
Cdd:cd19207     16 VGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGI-GCYMFRIDDFDVVDATMHGNAARFINHSC 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958702498 1717 QPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECL-GNGKTVCKCGAPNCSGFL 1774
Cdd:cd19207     95 EPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEdASNKLPCNCGAKRCRRFL 153

PHD4_NSD2

cd15657

PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1402-1442

7.12e-18

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: 78.89 E-value: 7.12e-18

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDCK 1442
Cdd:cd15657      1 WCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCR 41

PHD5_NSD3

cd15661

PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1814-1855

8.10e-18

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: 78.86 E-value: 8.10e-18

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1814 CFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 1855
Cdd:cd15661      2 CFQCGDGGELVMCDKKDCPKAYHLLCLNLTQPPYGKWECPWH 43

PHD1_NSD

cd15564

PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1238-1280

8.26e-18

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: 78.53 E-value: 8.26e-18

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1238 VCQNCEKLGELLLCEAQCCGAFHLECLGLTEMPRGKFICNECR 1280
Cdd:cd15564      1 VCQICEKPGKLLTCEGPCCGHFHLDCLGLSEQPDEPFKCDECT 43

PHD2_NSD2

cd15651

PHD finger 2 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1285-1331

1.09e-17

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: 78.35 E-value: 1.09e-17

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1285 TCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:cd15651      1 SCFVCKESKGDVKRCVVLHCGKFYHEACVRKYPLTVFENRGFRCPLH 47

PWWP

cd05162

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...

1451-1536

3.08e-17

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.

Pssm-ID: 438958 [Multi-domain] Cd Length: 86 Bit Score: 78.69 E-value: 3.08e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDvGEFPVLFFGSNDYLWTHQARVFPYmEGDVSSKDKMGKGVDGTYKKA 1530
Cdd:cd05162      2 DLVWAKLKGYPWWPARVVDPEELPEEVGKKKKK-GGVLVQFFGDNDYAWVKSKNIKPF-EEGFKKEFKKKKKKSKKFKKA 79


                   ....*.
gi 1958702498 1531 LQEAAA 1536
Cdd:cd05162     80 VEEAEE 85

SET

cd08161

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...

1637-1752

2.39e-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: 75.37 E-value: 2.39e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1637 VEIFRTLQRGWGLRTKTDIKKGEFVneyvgelideeecrariryaqehditnfymltldkdriidaGPkgnyARFMNHCC 1716
Cdd:cd08161      2 IRPSTIPGAGFGLFATRDIPKGEVI-----------------------------------------GL----ARFINHSC 36

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958702498 1717 QPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYN 1752
Cdd:cd08161     37 EPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDYG 72

SET_SETD5-like

cd10529

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...

1648-1752

2.95e-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: 2.95e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1648 GLRTKTDIKKGEFVNEYVGELIDEEECRARIRY---AQEHDItnFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQK 1724
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEVSLRSEFKEDNGFfkrPSPFVF--FYDGFEGLPLCVDARKYGNEARFIRRSCRPNAELRH 95

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958702498 1725 WSVNGDT-RVGLFALSDIKAGTELT--FNYN 1752
Cdd:cd10529     96 VVVSNGElRLFIFALKDIRKGTEITipFDYD 126

PHD2_NSD

cd15565

PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1285-1331

4.05e-16

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: 74.00 E-value: 4.05e-16

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958702498 1285 TCFVCKQSG---EDVKRCLLPLCGKFYHEECVQKYPPTVVQN-KGFRCPLH 1331
Cdd:cd15565      1 SCFVCKKLGsvgGEVFKCSVASCGKFYHEECLKKWPLTTISDsKKFRCPLH 51

SET_KMT2C

cd19208

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...

1636-1774

1.08e-15

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: 76.59 E-value: 1.08e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1636 DVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDiTNFYMLTLDKDRIIDAGPKGNYARFMNHC 1715
Cdd:cd19208     16 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQN-RGVYMFRIDNDHVIDATLTGGPARYINHS 94

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1716 CQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNG-KTVCKCGAPNCSGFL 1774
Cdd:cd19208     95 CAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNCRKWM 154

SET_KMT2D

cd19209

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...

1636-1774

1.82e-15

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: 75.89 E-value: 1.82e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1636 DVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDiTNFYMLTLDKDRIIDAGPKGNYARFMNHC 1715
Cdd:cd19209     17 NVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQN-RGIYMFRINNEHVIDATLTGGPARYINHS 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1716 CQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTV-CKCGAPNCSGFL 1774
Cdd:cd19209     96 CAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIpCHCGAWNCRKWM 155

PHD3_NSD

cd15566

PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1333-1385

6.74e-15

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: 70.54 E-value: 6.74e-15

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958702498 1333 CITCHAANPAnvsaSKGRLMRCVRCPVAYHANdfCLAAGSKILASNSIICPNH 1385
Cdd:cd15566      2 CATCEASGDG----SSGKLVRCIRCPRAYHAG--CIPAGSKLLNKKLIICPKH 48

PHD2_NSD3

cd15652

PHD finger 2 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1285-1331

3.40e-14

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: 68.74 E-value: 3.40e-14

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1285 TCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:cd15652      1 PCFSCKVPGKDVKRCSVNACGRFYHEACVRKYTTSAFESKGFRCPQH 47

PWWP

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...

19-106

3.58e-14

Pssm-ID: 459964 [Multi-domain] Cd Length: 92 Bit Score: 70.15 E-value: 3.58e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   19 GDLIWAKFKRRPWWPCRICSDPLINTHSKMKvanRRPYREYYVEAFGDpSEKAWVAGKAIVMFEGRHQFEELpvLRKRGK 98
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVLKP---KKKDGEYLVRFFGD-SEFAWVKPKDLKPFDEGDEFEYL--KKKKKK 74


                   ....*...
gi 1958702498   99 QKEKGYRH 106
Cdd:pfam00855   75 KKKKAFKK 82

PHD1_NSD3

cd15649

PHD finger 1 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1238-1280

3.22e-13

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: 65.56 E-value: 3.22e-13

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1238 VCQNCEKLGE-LLLCEAQCCGAFHLECLGLTEMPRGKFICNECR 1280
Cdd:cd15649      1 VCQVCESFGEsLVTCEGECCGLFHLECLGLTSLPDEKFICQECK 44

PHD1_AIRE

cd15539

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...

1403-1441

3.35e-13

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: 65.55 E-value: 3.35e-13

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLNID---IPEGNWYCNDC 1441
Cdd:cd15539      2 CAVCGDGGELLCCDGCPRAFHLACLVPPltlIPSGTWRCSSC 43

AWS

pfam17907

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...

1594-1632

3.44e-13

Pssm-ID: 465559 Cd Length: 39 Bit Score: 65.52 E-value: 3.44e-13

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1594 DENPCGIDSECINRMLLYECHPTVCPAGGRCQNQCFSKR 1632
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39

PHD2_CHD_II

cd15532

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1403-1441

8.82e-13

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: 64.61 E-value: 8.82e-13

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15532      2 CRVCKDGGELLCCDGCPSSYHLHCLNpplAEIPDGDWFCPRC 43

PHD3_NSD3

cd15655

PHD finger 3 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1346-1385

1.08e-12

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: 64.52 E-value: 1.08e-12

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1346 ASKGRLMRCVRCPVAYHANDFCLAAGSKILASNSIICPNH 1385
Cdd:cd15655     14 ASKGRMMRCLRCPVAYHTGDGCVAAGSVLVTPHIIICSNH 53

PWWP_AtATX3-like

cd20143

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...

1451-1534

6.89e-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: 63.93 E-value: 6.89e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEICHPRAVPSNIDKmRHDVGEFPVLFFG---SNDYLWTHQARVFPYMEGD--VSSKDKMGKGVDG 1525
Cdd:cd20143      4 DLVWAKVGTHPFWPARVVEPAEQAEEVRR-RCVPGSLCVYFFGpggSRDYGWVRRSMIFPFTDDLarFQTQKIKNKKRPQ 82


                   ....*....
gi 1958702498 1526 TYKKALQEA 1534
Cdd:cd20143     83 EFQEALEEA 91

PHD1_PHF12

cd15533

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...

1403-1441

3.77e-11

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: 59.68 E-value: 3.77e-11

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLN-----IDIPEGNWYCNDC 1441
Cdd:cd15533      2 CDSCGEGGDLLCCDRCPASFHLQCCNppldeEDLPPGEWLCHRC 45

AWS

smart00570

associated with SET domains; subdomain of PRESET

1584-1634

4.06e-11

associated with SET domains; subdomain of PRESET

Pssm-ID: 197795 Cd Length: 50 Bit Score: 60.11 E-value: 4.06e-11

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1958702498  1584 EIPRCNCKAT--DENPCGidSECINRMLLYEChPTVCPAGGRCQNQCFSKRQY 1634
Cdd:smart00570    1 DIMTCECKPTddDETACG--SDCLNRMLFIEC-SSSCPCGSYCSNQRFQKRQY 50

PHD5_NSD

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1402-1438

1.50e-10

Pssm-ID: 277043 [Multi-domain] Cd Length: 43 Bit Score: 58.11 E-value: 1.50e-10

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1402 WCFVCSEGGSLLCCD--SCPAAFHRECLNIDIPE-GNWYC 1438
Cdd:cd15568      1 ECFRCGDGGDLVLCDfkGCPKVYHLSCLGLEKPPgGKWIC 40

PWWP

cd05162

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...

19-105

2.42e-10

Pssm-ID: 438958 [Multi-domain] Cd Length: 86 Bit Score: 59.05 E-value: 2.42e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   19 GDLIWAKFKRRPWWPCRICSDPLINTHSKMKvanrRPYREYYVEAFGDpSEKAWVAGKAIVMFEgRHQFEELPVLRKRGK 98
Cdd:cd05162      1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKK----KKKGGVLVQFFGD-NDYAWVKSKNIKPFE-EGFKKEFKKKKKKSK 74


                   ....*..
gi 1958702498   99 QKEKGYR 105
Cdd:cd05162     75 KFKKAVE 81

PWWP_GLYR1

cd05836

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...

1451-1536

9.39e-10

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: 57.23 E-value: 9.39e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEICHPravPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEgdvsSKDKMGKGVDGT-YKK 1529
Cdd:cd05836      5 DLVWAKMKGFPPWPGKIVNP---PPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEE----FKEEMLKSKKSAgFKD 77


                   ....*..
gi 1958702498 1530 ALQEAAA 1536
Cdd:cd05836     78 AVEAIEE 84

PHD1_Rco1

cd15535

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...

1403-1441

1.32e-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: 55.50 E-value: 1.32e-09

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLNIDI-----PEGNWYCNDC 1441
Cdd:cd15535      2 CSACGGYGSFLCCDGCPRSFHFSCLDPPLeednlPDDEWFCNEC 45

PWWP_MSH6

cd05837

PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...

16-83

3.38e-09

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: 56.14 E-value: 3.38e-09

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958702498   16 YEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVANrrpyrEYYVEAFGDPSEKAWVAGKAIVMFEG 83
Cdd:cd05837      1 FSPGDLVWAKLEGYPWWPSLVCNHPTTGFHKKFGKKG-----EVHVQFFDDPPSRAWVKAKNVKPFTG 63

PHA03247

large tegument protein UL36; Provisional

1916-2288

4.34e-09

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 62.65 E-value: 4.34e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1916 PPTATLSPSPGtqqteqssemgtqgPKKSDQPPTDATQMlslSKKAVTGTCQRPllpERPPERTDSSShlldrirdlagS 1995
Cdd:PHA03247  2553 PPLPPAAPPAA--------------PDRSVPPPRPAPRP---SEPAVTSRARRP---DAPPQSARPRA-----------P 2601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1996 GTKSQSLVSSQRPQDRPPAKEGPRPQPPDRASPVTRPSSSPSVSSLPLERPLRMTEP---RLDKSIGAASPKSQAVEKPP 2072
Cdd:PHA03247  2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQ 2681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2073 APTglRLSSPDRLLN-TNSPKPQISDRPPDKSHASLTQRLPPPEKVLSAVVQSLVAkekalrPVDQNTQAKHRAAVVmDL 2151
Cdd:PHA03247  2682 RPR--RRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAL------PAAPAPPAVPAGPAT-PG 2752

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2152 IDLTPRQKERAASPQEVTAQADEKTPVLESSSRPT----SRGLGHVPRAVEKGGVSDPLQPPGKSAAPSEHPWQAVKSLT 2227
Cdd:PHA03247  2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT 2832

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 2228 HARFLSPPSAKAFLYESAIQASGRAPVGSEQTPGPPSPAPGLLK-----QVKQLSRGLTAKSGQSF 2288
Cdd:PHA03247  2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAaparpPVRRLARPAVSRSTESF 2898

SET_Suv4-20-like

cd10524

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...

1644-1756

7.75e-09

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: 56.52 E-value: 7.75e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1644 QRGWGLRTKTDIKKGEFVNEYVG---ELIDEEECRariryaQEHDITNFYMLT---LDKDRIIDaGPkgnyARFMNHCCQ 1717
Cdd:cd10524     17 HYGAKIIATKPIKKGEKIHELCGciaELSEEEEAL------LRPGGNDFSVMYssrKKCSQLWL-GP----AAFINHDCR 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1718 PNCetqKWSVNGDTRVGLFALSDIKAGTELTFNY--------NLECL 1756
Cdd:cd10524     86 PNC---KFVPTGKSTACVKVLRDIEPGEEITVYYgdnyfgenNEECE 129

PWWP_ZCWPW2

cd20146

PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...

15-106

1.00e-08

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: 55.38 E-value: 1.00e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   15 KYEVGDLIWAKFKRRPWWPCRICSDPLinTHSKMKVANRRPYREYYVEAFGDPSEKAWVAGKAIVMFEGRhqFEELPVLR 94
Cdd:cd20146      8 QLPLGSLVWAKMTGYPRWPAILTPDPI--CGEYVDYDEDGEVEKYHVEFLGKPHSHAWISAKSVEPYNSN--TKTPKCKT 83

                           90
                   ....*....|..
gi 1958702498   95 KRGKQKEKGYRH 106
Cdd:cd20146     84 KKSKKRKKSYES 95

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1402-1441

1.15e-08

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 52.98 E-value: 1.15e-08

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1958702498  1402 WCFVCSE---GGSLLCCDSCPAAFHRECLNI----DIPEGNWYCNDC 1441
Cdd:smart00249    1 YCSVCGKpddGGELLQCDGCDRWYHQTCLGPplleEEPDGKWYCPKC 47

SET_SpSET3-like

cd19183

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...

1636-1751

1.21e-08

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: 1.21e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1636 DVEIFRTLQRGW-GLRTKTDIKKGEFVNEYVGELIDEEECRAriryaqehDITNFY-MLTLDKDRI---------IDAGP 1704
Cdd:cd19183      2 EISSIGLANASRfGLFADRPIPAGDPIQELLGEIGLQSEYIA--------DPENQYqILGAPKPHVffhpqsplyIDTRR 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958702498 1705 KGNYARFMNHCCQPNCE--TQKWSVNGDTRVGLFALSDIKAGTELTFNY 1751
Cdd:cd19183     74 SGSVARFIRRSCRPNAElvTVASDSGSVLKFVLYASRDISPGEEITIGW 122

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1402-1442

2.42e-08

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 52.11 E-value: 2.42e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958702498 1402 WCFVCS---EGGSLLCCDSCPAAFHRECLNI-----DIPEGNWYCNDCK 1442
Cdd:pfam00628    1 YCAVCGksdDGGELVQCDGCDDWFHLACLGPpldpaEIPSGEWLCPECK 49

PHD_RSF1

cd15543

PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...

1403-1441

6.13e-08

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: 50.73 E-value: 6.13e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15543      5 CGLSDHPEWILLCDRCDAGYHTACLRpplMIIPDGNWFCPPC 46

PHD1_Lid2p_like

cd15519

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...

1403-1441

8.07e-08

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: 50.54 E-value: 8.07e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCS---EGGSLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15519      2 CEVCGlddNEGEVLLCDGCDAEYHTSCLDpplGEIPPGTWFCPSC 46

PHD4_NSD

cd15567

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1239-1279

9.13e-08

Pssm-ID: 277042 [Multi-domain] Cd Length: 41 Bit Score: 50.32 E-value: 9.13e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1239 CQNCEKLGELLLCEaQCCGAFHLECLGLTEMPRGKFICNEC 1279
Cdd:cd15567      2 CFICSEGGSLICCE-SCPASFHPECLGLEPPPEGKFYCEDC 41

PHD2_CHD_II

cd15532

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1814-1853

9.24e-08

Pssm-ID: 277007 [Multi-domain] Cd Length: 43 Bit Score: 50.36 E-value: 9.24e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1814 CFSCGDGGQLVSCKkpGCPKVYHADCLN--LTKRPAGKWECP 1853
Cdd:cd15532      2 CRVCKDGGELLCCD--GCPSSYHLHCLNppLAEIPDGDWFCP 41

SET_SMYD

cd20071

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...

1644-1751

9.72e-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: 52.77 E-value: 9.72e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1644 QRGWGLRTKTDIKKGEFVneyvgeLIDEEECRARIRYAQEHDITNFYMLTLDKdriidagpkgnYARFMNHCCQPNCEtq 1723
Cdd:cd20071      8 SKGRGLVATRDIEPGELI------LVEKPLVSVPSNSFSLTDGLNEIGVGLFP-----------LASLLNHSCDPNAV-- 68

                           90       100
                   ....*....|....*....|....*...
gi 1958702498 1724 kWSVNGDTRVGLFALSDIKAGTELTFNY 1751
Cdd:cd20071     69 -VVFDGNGTLRVRALRDIKAGEELTISY 95

PHD1_CHD_II

cd15531

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1402-1441

1.16e-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: 49.91 E-value: 1.16e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDI---PEGNWYCNDC 1441
Cdd:cd15531      1 YCEVCQQGGEIILCDTCPRAYHLVCLDPELekaPEGKWSCPHC 43

PHD4_NSD

cd15567

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1814-1852

1.45e-07

Pssm-ID: 277042 [Multi-domain] Cd Length: 41 Bit Score: 49.55 E-value: 1.45e-07

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1814 CFSCGDGGQLVSCKkpGCPKVYHADCLNLTKRPAGKWEC 1852
Cdd:cd15567      2 CFICSEGGSLICCE--SCPASFHPECLGLEPPPEGKFYC 38

PHD1_BPTF

cd15559

PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...

1403-1441

1.62e-07

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: 49.34 E-value: 1.62e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15559      2 CRVCHKLGDLLCCETCSAVYHLECVDpplEEVPEEDWQCEVC 43

PWWP

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

16-73

1.79e-07

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

Pssm-ID: 214603 [Multi-domain] Cd Length: 63 Bit Score: 50.04 E-value: 1.79e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958702498    16 YEVGDLIWAKFKRRPWWPCRICSDPLINTHskmKVANRRPYREYYVEAFGDPsEKAWV 73
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPKMTPDN---IMKRKSDENLYPVLFFGDK-DTAWI 54

PHD_TIF1gamma

cd15624

PHD finger found in transcriptional intermediary factor 1 gamma (TIF1gamma); TIF1gamma, also ...

1402-1442

4.98e-07

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: 48.12 E-value: 4.98e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHREC---LNIDIPEGNWYCNDCK 1442
Cdd:cd15624      1 WCAVCQNGGDLLCCEKCPKVFHLTChvpTLLSFPSGDWICTFCR 44

PHA03307

transcriptional regulator ICP4; Provisional

1947-2268

5.59e-07

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 55.18 E-value: 5.59e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1947 PPTDATQMLSLSKKAVTGTCQRPLLPERPPERTDSSShlldrirdLAGSGTKSQSLVSSQRPQDRPPAKEGPRPQPPDRA 2026
Cdd:PHA03307    53 VTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPT--------WSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2027 SP----VTRPSSSPSVSSLPLERPLRMTEPrldksIGAASPKSQAVEKPPAPTGLRLSSPDRLLNTNSPKPqiSDRPPDK 2102
Cdd:PHA03307   125 SPppspAPDLSEMLRPVGSPGPPPAASPPA-----AGASPAAVASDAASSRQAALPLSSPEETARAPSSPP--AEPPPST 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2103 SHASLTQRLPPPEKVLSAVVQSLVakekalrPVDQNTQAKHRAAVVMDliDLTPRQKERAASPQEVTAQADEKTPVLESS 2182
Cdd:PHA03307   198 PPAAASPRPPRRSSPISASASSPA-------PAPGRSAADDAGASSSD--SSSSESSGCGWGPENECPLPRPAPITLPTR 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2183 SRPTSRGLGHVPRAV---------EKGGVSDPlQPPGKSAAPSEHPwqavksltHARFLSPPSakaflyESAIQASGRAP 2253
Cdd:PHA03307   269 IWEASGWNGPSSRPGpasssssprERSPSPSP-SSPGSGPAPSSPR--------ASSSSSSSR------ESSSSSTSSSS 333

                          330
                   ....*....|....*
gi 1958702498 2254 VGSEQTPGPPSPAPG 2268
Cdd:PHA03307   334 ESSRGAAVSPGPSPS 348

PHD_TIF1alpha

cd15622

PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also ...

1402-1441

7.04e-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: 47.75 E-value: 7.04e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHREC---LNIDIPEGNWYCNDC 1441
Cdd:cd15622      1 WCAVCQNGGELLCCEKCPKVFHLSChvpTLMNFPSGEWICTFC 43

PHD_TIF1_like

cd15541

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...

1402-1441

7.42e-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: 7.42e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHREClNI----DIPEGNWYCNDC 1441
Cdd:cd15541      1 WCAVCQNGGELLCCDKCPRVFHLDC-HIppipEFPSGEWSCSLC 43

PHD5_NSD

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1238-1276

1.01e-06

Pssm-ID: 277043 [Multi-domain] Cd Length: 43 Bit Score: 47.32 E-value: 1.01e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1238 VCQNCEKLGELLLCEAQCCG-AFHLECLGLTEMPRGKFIC 1276
Cdd:cd15568      1 ECFRCGDGGDLVLCDFKGCPkVYHLSCLGLEKPPGGKWIC 40

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1403-1441

1.10e-06

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: 47.31 E-value: 1.10e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1403 CFVCSEGG----SLLCCDSCPAAFHRECLNID----IPEGNWYCNDC 1441
Cdd:cd15489      2 CIVCGKGGdlggELLQCDGCGKWFHADCLGPPlssfVPNGKWICPVC 48

PHD_TIF1delta

cd15625

PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta); TIF1delta, also ...

1399-1442

1.33e-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: 1.33e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1399 NVSWCFVCSEGGSLLCCDSCPAAFHREC---LNIDIPEGNWYCNDCK 1442
Cdd:cd15625      1 NEDFCAVCLNGGELLCCDRCPKVFHLSChvpALLSFPVGEWVCTLCR 47

PWWP_ZCWPW1

cd20145

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...

15-108

1.57e-06

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: 49.08 E-value: 1.57e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   15 KYEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVANRRPYReYYVEAFGDPSEKAWVAGKAIvmfegrHQFEELPVLR 94
Cdd:cd20145      5 KYTPGSLVWAKMPGYPWWPAMVEDDPDTEEFFWLDEESDIPTK-YHVTFFDKPVSRAWVRASSI------KPFTDNSNEP 77

                           90
                   ....*....|....
gi 1958702498   95 KRGKQKEKGYRHKV 108
Cdd:cd20145     78 NLTKKKGKKYKKRL 91

SET_ATXR5_6-like

cd10539

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...

1654-1752

1.65e-06

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: 49.72 E-value: 1.65e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1654 DIKKGEFVNEYVGElIDEEECRariryaqEHDITNFYMLTL-----DKDRIIDAGPKGNYARFM----NHCCQ----PNC 1720
Cdd:cd10539     23 FIKDLTIIAEYTGD-VDYIRNR-------EFDDNDSIMTLLlagdpSKSLVICPDKRGNIARFIsginNHTKDgkkkQNC 94

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958702498 1721 ETQKWSVNGDTRVGLFALSDIKAGTELTFNYN 1752
Cdd:cd10539     95 KCVRYSINGEARVLLVATRDIAKGERLYYDYN 126

PWWP_ScIOC4-like

cd05840

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...

1450-1534

1.71e-06

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

Pssm-ID: 438965 Cd Length: 94 Bit Score: 48.07 E-value: 1.71e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1450 REIVWVKVGRYRWWPAEICHPRAVPSNIDKM-----RHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVD 1524
Cdd:cd05840      1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLKAkkrkpKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                           90
                   ....*....|
gi 1958702498 1525 GTYKKALQEA 1534
Cdd:cd05840     81 KDLIEAYEVA 90

SET_SpSet7-like

cd10540

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...

1636-1752

2.41e-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: 48.40 E-value: 2.41e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1636 DVEIFRTLQRGWGLRTKTDIKKGEFVneyvgelideEECRArIRYAQE---HDITnfymlTLDKDRIIdAGPKGNYARFM 1712
Cdd:cd10540      1 RLEVKPSTLKGRGVFATRPIKKGEVI----------EEAPV-IVLPKEeyqHLCK-----TVLDHYVF-SWGDGCLALAL 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958702498 1713 ------NHCCQPNCEtqKWSVNGDTRVGLFALSDIKAGTELTFNYN 1752
Cdd:cd10540     64 gygsmfNHSYTPNAE--YEIDFENQTIVFYALRDIEAGEELTINYG 107

PHD1_AIRE

cd15539

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...

1813-1852

2.91e-06

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 45.90 E-value: 2.91e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1813 ECFSCGDGGQLVSCKkpGCPKVYHADCLN--LTKRPAGKWEC 1852
Cdd:cd15539      1 ECAVCGDGGELLCCD--GCPRAFHLACLVppLTLIPSGTWRC 40

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1238-1279

5.99e-06

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 45.28 E-value: 5.99e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1958702498  1238 VCQNCEKLGELLLCEaQCCGAFHLECLGLT---EMPRGKFICNEC 1279
Cdd:smart00249    4 VCGKPDDGGELLQCD-GCDRWYHQTCLGPPlleEEPDGKWYCPKC 47

PHD_PRKCBP1

cd15538

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...

1403-1441

1.19e-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: 44.24 E-value: 1.19e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLNIDI-PEGNWYCNDC 1441
Cdd:cd15538      2 CWRCHKEGQVLCCSLCPRVYHKKCLKLTSePDEDWVCPEC 41

PHD_BAZ1A

cd15627

PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...

1403-1441

1.41e-05

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: 44.31 E-value: 1.41e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEGG---SLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15627      2 CRICRRKGdaeKMLLCDGCDRGHHMYCLRpplKKVPEGDWFCPDC 46

PHD5_NSD3

cd15661

PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1402-1438

1.74e-05

Pssm-ID: 277131 Cd Length: 43 Bit Score: 43.80 E-value: 1.74e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1402 WCFVCSEGGSLLCCDS--CPAAFHRECLNIDIPE-GNWYC 1438
Cdd:cd15661      1 YCFQCGDGGELVMCDKkdCPKAYHLLCLNLTQPPyGKWEC 40

PHD_BRPF_JADE_like

cd15492

PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; ...

1403-1441

1.95e-05

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: 43.76 E-value: 1.95e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEGGS-----LLCCDSCPAAFHRECLNID-IPEGNWYCNDC 1441
Cdd:cd15492      2 CDVCLDGESeddneIVFCDGCNVAVHQSCYGIPlIPEGDWFCRKC 46

PHD_PHF21A

cd15523

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...

1403-1441

2.13e-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: 43.54 E-value: 2.13e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15523      2 CSVCRKSGELLMCDTCSLVYHLDCLDpplKTIPKGMWICPKC 43

PHD_BAZ2A_like

cd15545

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...

1403-1441

2.56e-05

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: 43.45 E-value: 2.56e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEG---GSLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15545      2 CQICRSGdneDQLLLCDGCDRGYHTYCFKpkmTNVPEGDWFCPEC 46

SET_SETD5

cd19181

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...

1649-1770

2.66e-05

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: 46.54 E-value: 2.66e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1649 LRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQE-HDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWSV 1727
Cdd:cd19181     21 LRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRpYPFVLFYSKFNGVEMCVDARTFGNDARFIRRSCTPNAEVRHMIA 100

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1728 NGDTRVGLFALSDIKAGTELTFNYNLE---ClgNGKTVCKC--GAPNC 1770
Cdd:cd19181    101 DGMIHLCIYAVAAIAKDAEVTIAFDYEysnC--NYKVDCAChkGNRNC 146

PHD4_NSD3

cd15658

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1239-1279

2.83e-05

Pssm-ID: 277128 Cd Length: 40 Bit Score: 42.98 E-value: 2.83e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1239 CQNCEKLGELLLCEAqCCGAFHLECLGLtEMPRGKFICNEC 1279
Cdd:cd15658      2 CFVCARGGRLLCCES-CPASFHPECLSI-EMPEGCWNCNEC 40

PHD2_KAT6A_6B

cd15527

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...

1403-1441

3.51e-05

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: 43.14 E-value: 3.51e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEGG---SLLCCDSCPAAFHRECLNIDI---PEGNWYCNDC 1441
Cdd:cd15527      2 CSVCQDSGnadNLLFCDACDKGFHMECHDPPLtrmPKGKWVCQIC 46

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1238-1280

3.60e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 43.25 E-value: 3.60e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1238 VCQNCEKLGELLLCEaQCCGAFHLECLGLT----EMPRGKFICNECR 1280
Cdd:pfam00628    4 VCGKSDDGGELVQCD-GCDDWFHLACLGPPldpaEIPSGEWLCPECK 49

PHD_Phf1p_Phf2p_like

cd15502

PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 ...

1403-1441

4.36e-05

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: 42.81 E-value: 4.36e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958702498 1403 CFVCSEGGS-----LLCCDSCPAAFHRECLN-------IDIPEGNWYCNDC 1441
Cdd:cd15502      2 CIVCQRGHSpksnrIVFCDGCNTPYHQLCHDpsiddevVEDPDAEWFCKKC 52

PHD_PRKCBP1

cd15538

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...

1814-1853

5.17e-05

Pssm-ID: 277013 Cd Length: 41 Bit Score: 42.31 E-value: 5.17e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958702498 1814 CFSCGDGGQLVSCKKpgCPKVYHADCLNLTKRPAGKWECP 1853
Cdd:cd15538      2 CWRCHKEGQVLCCSL--CPRVYHKKCLKLTSEPDEDWVCP 39

PWWP_PWWP2B

cd20153

PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...

18-117

5.33e-05

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: 44.56 E-value: 5.33e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   18 VGDLIWAKFKRRPWWPCRICSdplINTHSKmkvANRRP-YREYYVEAFGDPSEKAWVAGKA---IVMFEGRHQFEELPVL 93
Cdd:cd20153     16 VGDIVWGKIHGFPWWPARVLS---ISLSQK---EDGEPsWQEAKVSWFGSPTTSLLSVSKLspfSEFFKLRFNRKKKGMY 89

                           90       100
                   ....*....|....*....|....*.
gi 1958702498   94 RKRGKQKEKGYRHKVP--QKILSKWE 117
Cdd:cd20153     90 RKAITEAAKAAEHLTPeiRELLTQFE 115

SET_KMT5C

cd19185

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...

1649-1765

5.71e-05

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) and similar proteins; KMT5C (also termed lysine N-methyltransferase 5C, lysine-specific methyltransferase 5C, suppressor of variegation 4-20 homolog 2, Su(var)4-20 homolog 2 or Suv4-20h2) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.

Pssm-ID: 380962 Cd Length: 142 Bit Score: 45.42 E-value: 5.71e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1649 LRTKTDIKKGEFVNEYVGELIDEEECRARiryAQEHDITNFYMlTLDKDRIIDAGPkgnyARFMNHCCQPNCETQkwSVN 1728
Cdd:cd19185     25 TRAWKKNEKLELLVGCIAELREEDEGLLR---AGENDFSIMYS-TRKRSAQLWLGP----AAFINHDCKPNCKFV--PAD 94

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958702498 1729 GDTRVgLFALSDIKAGTELTFNYNLECLGNGKTVCKC 1765
Cdd:cd19185     95 GNAAC-VKVLRDIEPGDEVTCFYGEGFFGEKNEHCEC 130

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1814-1855

5.74e-05

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 42.58 E-value: 5.74e-05

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1958702498  1814 CFSCG---DGGQLVSCKkpGCPKVYHADCLNLTKR---PAGKWECPWH 1855
Cdd:smart00249    2 CSVCGkpdDGGELLQCD--GCDRWYHQTCLGPPLLeeePDGKWYCPKC 47

PHD1_PHF12

cd15533

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...

1814-1857

5.91e-05

Pssm-ID: 277008 [Multi-domain] Cd Length: 45 Bit Score: 42.34 E-value: 5.91e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1814 CFSCGDGGQLVSCKKpgCPKVYHADCLN----LTKRPAGKWECpwHQC 1857
Cdd:cd15533      2 CDSCGEGGDLLCCDR--CPASFHLQCCNppldEEDLPPGEWLC--HRC 45

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1285-1331

7.71e-05

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 42.30 E-value: 7.71e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1285 TCFVCKQSGEDVKRCLL-PLCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:cd15489      1 SCIVCGKGGDLGGELLQcDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48

PHD1_AIRE

cd15539

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...

1239-1279

8.54e-05

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 41.67 E-value: 8.54e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1239 CQNCEKLGELLLCEAqCCGAFHLECLG--LTEMPRGKFICNEC 1279
Cdd:cd15539      2 CAVCGDGGELLCCDG-CPRAFHLACLVppLTLIPSGTWRCSSC 43

PHD2_KAT6A_6B

cd15527

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...

1238-1279

9.94e-05

Pssm-ID: 277002 Cd Length: 46 Bit Score: 41.59 E-value: 9.94e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1238 VCQNCEKLGELLLCEAqCCGAFHLECLG--LTEMPRGKFICNEC 1279
Cdd:cd15527      4 VCQDSGNADNLLFCDA-CDKGFHMECHDppLTRMPKGKWVCQIC 46

PWWP_BS69-like

cd05841

PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar ...

1446-1542

1.04e-04

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

Pssm-ID: 438966 Cd Length: 89 Bit Score: 43.15 E-value: 1.04e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1446 KPHyrEIVWVKVGRYRWWPAEIchpravpsnidkMRHDVGEFPVLFFGSNDYLWT-------HQARVFPYMEGDVSSKDK 1518
Cdd:cd05841      5 VVH--PLVWVKLDGFPFWPAKV------------MGTKDGQVDVRFFGDYDRAWLpsknvtlHTREIVSTLPDSSESKDK 70

                           90       100
                   ....*....|....*....|....
gi 1958702498 1519 MgkgvdgTYKKALQEAAARFEELK 1542
Cdd:cd05841     71 R------TLKKAIKELERHIALLR 88

PWWP_HRP

cd05834

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...

16-40

1.21e-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: 42.54 E-value: 1.21e-04

                           10        20
                   ....*....|....*....|....*
gi 1958702498   16 YEVGDLIWAKFKRRPWWPCRICSDP 40
Cdd:cd05834      1 FKPGDLVFAKVKGYPPWPARIDEIP 25

PWWP_PWWP2A

cd20152

PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...

1451-1547

1.37e-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: 43.84 E-value: 1.37e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEIChpravpsNIDKMRHDVG-----EFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVdg 1525
Cdd:cd20152     24 DIVWAKIYGFPWWPARIL-------AITVSRKDNGllvrqEARISWFGSPTTSFLALSQLAPFLENFQSRFNKKRKGL-- 94

                           90       100
                   ....*....|....*....|..
gi 1958702498 1526 tYKKALQEAAarfeelKAQKEL 1547
Cdd:cd20152     95 -YRKAITEAA------KAAKQL 109

PHD_BS69

cd15537

PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing ...

1402-1441

1.38e-04

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: 41.18 E-value: 1.38e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGN---WYCNDC 1441
Cdd:cd15537      1 YCFECHAPGEVLPCSGCFRVYHSDCLSEDFRPDStshWTCPVC 43

PHD_ING3

cd15585

PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also ...

1821-1857

1.39e-04

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: 41.28 E-value: 1.39e-04

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958702498 1821 GQLVSCKKPGCP-KVYHADCLNLTKRPAGKWECPwhQC 1857
Cdd:cd15585     10 GEMVGCDNDDCPiEWFHYGCVGLTEAPKGKWYCP--QC 45

PWWP_GLYR1

cd05836

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...

16-82

1.55e-04

Pssm-ID: 438961 [Multi-domain] Cd Length: 86 Bit Score: 42.59 E-value: 1.55e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958702498   16 YEVGDLIWAKFKRRPWWPCRICSDPLinthSKMKVANRRPYreYYVEAFGdpSEK-AWVAGKAIVMFE 82
Cdd:cd05836      1 FKIGDLVWAKMKGFPPWPGKIVNPPP----DLKKPPRKKKM--HCVYFFG--SENyAWIEDENIKPYE 60

PHD1_BPTF

cd15559

PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...

1239-1279

1.62e-04

Pssm-ID: 277034 [Multi-domain] Cd Length: 43 Bit Score: 40.86 E-value: 1.62e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1239 CQNCEKLGELLLCEAqCCGAFHLECLG--LTEMPRGKFICNEC 1279
Cdd:cd15559      2 CRVCHKLGDLLCCET-CSAVYHLECVDppLEEVPEEDWQCEVC 43

Atrophin-1

pfam03154

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...

1922-2265

2.36e-04

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 46.68 E-value: 2.36e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1922 SPS-PGTQQTEQSSEMGTQGPKKSDQPPTDATQ--MLSLSKKAVTGTCQR------PLLPERPPERTDSSSHLLDRIRDL 1992
Cdd:pfam03154  145 SPSiPSPQDNESDSDSSAQQQILQTQPPVLQAQsgAASPPSPPPPGTTQAatagptPSAPSVPPQGSPATSQPPNQTQST 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1993 AGSGTKSQSLVS--SQR-PQDRPPAKEGPRPQPPDRASPVTRPSSSPSVSSLPLERPLR-----MTEPRLDKSIGAASPK 2064
Cdd:pfam03154  225 AAPHTLIQQTPTlhPQRlPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQtgpshMQHPVPPQPFPLTPQS 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2065 SQAvEKPPAPTGlrlsspdrllNTNSPKPQISDRPPDKSHASLTQrlPPPEKVLSAVVQSLV-AKEKALRPVDQ--NTQA 2141
Cdd:pfam03154  305 SQS-QVPPGPSP----------AAPGQSQQRIHTPPSQSQLQSQQ--PPREQPLPPAPLSMPhIKPPPTTPIPQlpNPQS 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2142 -KHRAAVvmdlidltprqkeRAASPQEVTAQADEKTPVLESSSRPTSRGLGHVPRAVEKGGVSDPLQPPgksaaPSEHPw 2220
Cdd:pfam03154  372 hKHPPHL-------------SGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPP-----PAQPP- 432

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 2221 qavkSLTHARFLSPPSAkaflyeSAIQASGRAPVGSeQTPGPPSP 2265
Cdd:pfam03154  433 ----VLTQSQSLPPPAA------SHPPTSGLHQVPS-QSPFPQHP 466

PWWP_DNMT3

cd05835

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...

17-60

2.53e-04

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: 41.86 E-value: 2.53e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958702498   17 EVGDLIWAKFKRRPWWPCRI-----CSDPLI------------NTHSKMKVANRRPYREYY 60
Cdd:cd05835      1 KIGDLVWAKLKGSPWWPGIVvshkdCGQKPPaegsvwvfwfgdHKVSEVPLDKILPFAEFF 61

PHD5_NSD2

cd15660

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1239-1276

2.56e-04

Pssm-ID: 277130 Cd Length: 43 Bit Score: 40.69 E-value: 2.56e-04

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1239 CQNCEKLGELLLCEAQ-CCGAFHLECLGLTEMPRGKFIC 1276
Cdd:cd15660      2 CFRCGDGGQLVLCDRKsCTKAYHLSCLGLTKRPFGKWEC 40

PHD_TIF1_like

cd15541

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...

1813-1852

2.93e-04

Pssm-ID: 277016 [Multi-domain] Cd Length: 43 Bit Score: 40.41 E-value: 2.93e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1813 ECFSCGDGGQLVSCKKpgCPKVYHADCL--NLTKRPAGKWEC 1852
Cdd:cd15541      1 WCAVCQNGGELLCCDK--CPRVFHLDCHipPIPEFPSGEWSC 40

PWWP_PWWP2

cd20140

PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...

18-60

2.97e-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: 41.86 E-value: 2.97e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958702498   18 VGDLIWAKFKRRPWWPCRICS-------DPLI------------NTHSKMKVANRRPYREYY 60
Cdd:cd20140      6 VGDIVWGKIHGFPWWPGRILSitvsrddNGELstqeahvswfgsSTTSYMPCSQLYPFLEDF 67

PWWP_NSD_rpt1

cd20144

first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1451-1570

2.97e-04

Pssm-ID: 438972 Cd Length: 114 Bit Score: 42.30 E-value: 2.97e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEIC-------HPRAVPSNIDKMRhdvgEFPVLFFGSND-YLWTHQARVFPYmEGdvssKDKmgkg 1522
Cdd:cd20144      3 DLVWAKVSGHPWWPCMVTydpesglYTKIKGSGGRTYR----QYHVQFFGDNGeRGWVSEKSLMPF-EG----KEK---- 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1523 vdgtykkalqeaaarFEELKAqkelRQLQEDRKNDKKPPPYKHIKVNR 1570
Cdd:cd20144     70 ---------------FEELVK----ELKKKAKKKSKKAKLEKKVKPSR 98

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1814-1855

3.24e-04

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 40.38 E-value: 3.24e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958702498 1814 CFSCGDGGQ----LVSCKKpgCPKVYHADCLNLTKR---PAGKWECPWH 1855
Cdd:cd15489      2 CIVCGKGGDlggeLLQCDG--CGKWFHADCLGPPLSsfvPNGKWICPVC 48

PWWP_HRP

cd05834

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...

1451-1534

3.58e-04

Pssm-ID: 438959 [Multi-domain] Cd Length: 82 Bit Score: 41.38 E-value: 3.58e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEICHPrAVPSNIDKmrhdvGEFPVLFFGSNDY--LWTHQarVFPYMEgdvsSKDKMGKgvdGTYK 1528
Cdd:cd05834      5 DLVFAKVKGYPPWPARIDEI-PEGAKIPK-----NKYPVFFYGTHETafLKPKD--LFPYEE----NKEKYGK---PRKR 69


                   ....*.
gi 1958702498 1529 KALQEA 1534
Cdd:cd05834     70 KGFNEG 75

PHD_BRPF2

cd15677

PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar ...

1403-1441

3.73e-04

PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; BRPF2, also termed bromodomain-containing protein 1 (BRD1), or BR140-like protein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. This model corresponds to the canonical Cys4HisCys3 PHD finger.

Pssm-ID: 277147 [Multi-domain] Cd Length: 54 Bit Score: 40.38 E-value: 3.73e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEGGS-----LLCCDSCPAAFHRECLNID-IPEGNWYCNDC 1441
Cdd:cd15677      4 CCICMDGECqnsnvILFCDMCNLAVHQECYGVPyIPEGQWLCRHC 48

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1238-1279

3.87e-04

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 39.99 E-value: 3.87e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958702498 1238 VCQNCEK----LGELLLCEaQCCGAFHLECLGLTE---MPRGKFICNEC 1279
Cdd:cd15489      1 SCIVCGKggdlGGELLQCD-GCGKWFHADCLGPPLssfVPNGKWICPVC 48

PWWP_AtATX3-like

cd20143

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...

17-105

4.18e-04

Pssm-ID: 438971 [Multi-domain] Cd Length: 100 Bit Score: 41.59 E-value: 4.18e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498   17 EVGDLIWAKFKRRPWWPCRICsDPlinthSKMKVANRRPYR--EYYVEAFGDPSEK--AWVAGKAIVMFegrhqFEELPV 92
Cdd:cd20143      1 VEGDLVWAKVGTHPFWPARVV-EP-----AEQAEEVRRRCVpgSLCVYFFGPGGSRdyGWVRRSMIFPF-----TDDLAR 69

                           90
                   ....*....|....*.
gi 1958702498   93 L---RKRGKQKEKGYR 105
Cdd:cd20143     70 FqtqKIKNKKRPQEFQ 85

PWWP_ZCWPW2

cd20146

PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...

1451-1553

4.29e-04

Pssm-ID: 438974 Cd Length: 113 Bit Score: 41.90 E-value: 4.29e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEIChprAVPSNIDKMRHDVGEFP----VLFFGSN-DYLWTHQARVFPYMEG--DVSSKDKMGKGV 1523
Cdd:cd20146     13 SLVWAKMTGYPRWPAILT---PDPICGEYVDYDEDGEVekyhVEFLGKPhSHAWISAKSVEPYNSNtkTPKCKTKKSKKR 89

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958702498 1524 DGTYKKALQEAaarfeelkaqKELRQLQED 1553
Cdd:cd20146     90 KKSYESALEEA----------ERLLKLTCE 109

PHD_Yng1p_like

cd15587

PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the ...

1246-1279

4.39e-04

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: 40.09 E-value: 4.39e-04

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958702498 1246 GELLLCEAQCCGA--FHLECLGLTEMPRGKFICNEC 1279
Cdd:cd15587     10 GEMVACDNPDCKIewFHFECVGLTETPKGKWYCSDC 45

PHD1_PHF12

cd15533

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...

1238-1279

4.43e-04

Pssm-ID: 277008 [Multi-domain] Cd Length: 45 Bit Score: 40.03 E-value: 4.43e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958702498 1238 VCQNCEKLGELLLCEaQCCGAFHLEC----LGLTEMPRGKFICNEC 1279
Cdd:cd15533      1 YCDSCGEGGDLLCCD-RCPASFHLQCcnppLDEEDLPPGEWLCHRC 45

ADDz_Dnmt3

cd11725

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...

1814-1853

4.59e-04

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: 41.61 E-value: 4.59e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1814 CFSCGDGGQLVSCKKPGCPKVYHADCLNL--------TKRPAGKWECP 1853
Cdd:cd11725     50 CTICGGGGEVVLCDNPDCTRVYCTECLDLllgpgavaKILESDPWFCF 97

PHD4_NSD2

cd15657

PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1239-1280

4.96e-04

Pssm-ID: 277127 Cd Length: 41 Bit Score: 39.60 E-value: 4.96e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1239 CQNCEKLGELLLCEAqCCGAFHLECLGLtEMPRGKFICNECR 1280
Cdd:cd15657      2 CFVCSKGGSLLCCES-CPAAFHPDCLNI-EMPDGSWFCNDCR 41

PHD_Yng1p_like

cd15587

PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the ...

1821-1853

5.03e-04

Pssm-ID: 277062 [Multi-domain] Cd Length: 47 Bit Score: 39.71 E-value: 5.03e-04

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958702498 1821 GQLVSCKKPGCP-KVYHADCLNLTKRPAGKWECP 1853
Cdd:cd15587     10 GEMVACDNPDCKiEWFHFECVGLTETPKGKWYCS 43

PHD1_CHD_II

cd15531

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1814-1853

5.39e-04

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 39.51 E-value: 5.39e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1814 CFSCGDGGQLVSCKKpgCPKVYHADCLN--LTKRPAGKWECP 1853
Cdd:cd15531      2 CEVCQQGGEIILCDT--CPRAYHLVCLDpeLEKAPEGKWSCP 41

PWWP_MSH6

cd05837

PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...

1451-1534

5.39e-04

Pssm-ID: 438962 Cd Length: 103 Bit Score: 41.50 E-value: 5.39e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEIC-HPRavpSNIDKMRHDVGEFPVLFFG---SNDylWTHQARVFPYMEGDvsSKDKMGKGV--- 1523
Cdd:cd05837      5 DLVWAKLEGYPWWPSLVCnHPT---TGFHKKFGKKGEVHVQFFDdppSRA--WVKAKNVKPFTGSD--DKEFQKGGMffs 77

                           90
                   ....*....|..
gi 1958702498 1524 -DGTYKKALQEA 1534
Cdd:cd05837     78 kDPKWKKAVKEA 89

PWWP_ZCWPW1

cd20145

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...

1452-1545

5.41e-04

Pssm-ID: 438973 Cd Length: 115 Bit Score: 41.77 E-value: 5.41e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1452 IVWVKVGRYRWWPA--EIChpravpsnidkmrHDVGEF---------P----VLFFGSN-DYLWTHQARVFPYMEGDVSS 1515
Cdd:cd20145     11 LVWAKMPGYPWWPAmvEDD-------------PDTEEFfwldeesdiPtkyhVTFFDKPvSRAWVRASSIKPFTDNSNEP 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958702498 1516 KDKMGKGVDgtYKKALQEAAARFEElkAQK 1545
Cdd:cd20145     78 NLTKKKGKK--YKKRLNEAVEMARE--ALK 103

PWWP_DNMT3

cd05835

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...

1451-1537

5.58e-04

Pssm-ID: 438960 [Multi-domain] Cd Length: 89 Bit Score: 41.09 E-value: 5.58e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1451 EIVWVKVGRYRWWPAEICHPRAV---PSNIDKMRhdvgefpVLFFGSNDYLWTHQARVFPYMEGDVS-SKDKMGKgvdGT 1526
Cdd:cd05835      4 DLVWAKLKGSPWWPGIVVSHKDCgqkPPAEGSVW-------VFWFGDHKVSEVPLDKILPFAEFFNKfYISKNSS---KL 73

                           90
                   ....*....|....*
gi 1958702498 1527 YKK----ALQEAAAR 1537
Cdd:cd05835     74 YKKavyeALKEAAER 88

PHA03321

tegument protein VP11/12; Provisional

1990-2281

5.71e-04

tegument protein VP11/12; Provisional

Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 45.33 E-value: 5.71e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1990 RDLAGSGTKSQ------SLVSSQRPQDRPPAKEGPRPQPPDRAspvtRPSSSPSVSSLPLERPLRMTEPRLDKSIGAASP 2063
Cdd:PHA03321   406 TELFRTGVPSEhyeaslRLLSSRQPPGAPAPRRDNDPPPPPRA----RPGSTPACARRARAQRARDAGPEYVDPLGALRR 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2064 KSQAVEKPPAPTGLRlSSPDRLLNTNSPKPqisdRPPDKSHASLTQR---LPPPEkvlsAVVQSLVAKEkaLRPVDQNTQ 2140
Cdd:PHA03321   482 LPAGAAPPPEPAAAP-SPATYYTRMGGGPP----RLPPRNRATETLRpdwGPPAA----APPEQMEDPY--LEPDDDRFD 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2141 AKHRAAvvmdlidltprqkeRAASPQEVTAQADEKTPVLESSSR---------PTSRGLGHV-PRAVEKGGVSDPLQPPG 2210
Cdd:PHA03321   551 RRDGAA--------------AAATSHPREAPAPDDDPIYEGVSDseepvyeeiPTPRVYQNPlPRPMEGAGEPPDLDAPT 616

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2211 KSAAPSEHPwqaVKSLTHARFLSPPSakaflyesaiqASGRAPVGSEQTPGPPS-----PAPGLLK-----QVKQLSRGL 2280
Cdd:PHA03321   617 SPWVEEENP---IYGWGDSPLFSPPP-----------AARFPPPDPALSPEPPAlpahrPRPGALApdgpaNLAALSAML 682


                   .
gi 1958702498 2281 T 2281
Cdd:PHA03321   683 T 683

PHD_ING5

cd15685

PHD finger found in inhibitor of growth protein 5 (ING5); ING5, also termed p28ING5, is one ...

1821-1853

6.01e-04

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: 39.65 E-value: 6.01e-04

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958702498 1821 GQLVSCKKPGCP-KVYHADCLNLTKRPAGKWECP 1853
Cdd:cd15685     11 GEMIGCDNPDCPiEWFHFACVDLTTKPKGKWFCP 44

PHD_BRPF

cd15572

PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF ...

1403-1441

6.82e-04

PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a 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. This model corresponds to the canonical Cys4HisCys3 PHD finger.

Pssm-ID: 277047 [Multi-domain] Cd Length: 54 Bit Score: 39.52 E-value: 6.82e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEG-----GSLLCCDSCPAAFHRECLNID-IPEGNWYCNDC 1441
Cdd:cd15572      4 CCICLDGecqnsNVILFCDMCNLAVHQECYGVPyIPEGQWLCRRC 48

PHD4_NSD3

cd15658

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1814-1852

7.41e-04

Pssm-ID: 277128 Cd Length: 40 Bit Score: 39.13 E-value: 7.41e-04

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1814 CFSCGDGGQLVSCKkpGCPKVYHADCLNLtKRPAGKWEC 1852
Cdd:cd15658      2 CFVCARGGRLLCCE--SCPASFHPECLSI-EMPEGCWNC 37

SET_KMT2E

cd19182

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...

1649-1754

7.72e-04

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: 41.80 E-value: 7.72e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1649 LRTKTDIKKGEFVNEYVGELIDEEECRAR-IRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWSV 1727
Cdd:cd19182     21 LKAAKDLPPDTLIIEYRGKFMLREQFEANgYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHVIE 100

                           90       100
                   ....*....|....*....|....*..
gi 1958702498 1728 NGDTRVGLFALSDIKAGTELTFNYNLE 1754
Cdd:cd19182    101 DGTIHLYIYSIRSIPKGTEITIAFDFD 127

PHD5_NSD1

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1403-1438

7.73e-04

Pssm-ID: 277129 Cd Length: 43 Bit Score: 39.16 E-value: 7.73e-04

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1403 CFVCSEGGSLLCCDS--CPAAFHRECLNIDI-PEGNWYC 1438
Cdd:cd15659      2 CFSCGDGGQLVSCKKpgCPKVYHADCLNLTKrPAGKWEC 40

PHD_ING4_5

cd15586

PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed ...

1821-1853

7.98e-04

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: 39.09 E-value: 7.98e-04

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958702498 1821 GQLVSCKKPGCP-KVYHADCLNLTKRPAGKWECP 1853
Cdd:cd15586     10 GEMIGCDNPDCPiEWFHFACVGLTTKPKGKWFCP 43

PWWP_NSD3_rpt1

cd20163

first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...

1451-1508

8.26e-04

Pssm-ID: 438991 Cd Length: 130 Bit Score: 41.46 E-value: 8.26e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958702498 1451 EIVWVKVGRYRWWPAEI-CHPRA-VPSNIDKmrHDVGEFPVLFFGSN-DYLWTHQARVFPY 1508
Cdd:cd20163      5 DLVWSKVGTYPWWPCMVsSDPQLeVHTKINT--RGAREYHVQFFSSQpERAWVHEKRVREY 63

PHD5_NSD

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1286-1331

8.49e-04

Pssm-ID: 277043 [Multi-domain] Cd Length: 43 Bit Score: 38.85 E-value: 8.49e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958702498 1286 CFVCKQsGEDVKRCLLPLCGKFYHEECVQKyppTVVQNKGFRCPLH 1331
Cdd:cd15568      2 CFRCGD-GGDLVLCDFKGCPKVYHLSCLGL---EKPPGGKWICPWH 43

PHD_PHRF1

cd15536

PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also ...

1403-1441

8.87e-04

PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also termed KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase that induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a RING finger.

Pssm-ID: 277011 Cd Length: 46 Bit Score: 38.93 E-value: 8.87e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECLNID---IPEGNWYCNDC 1441
Cdd:cd15536      5 CGRSDREDRLLLCDGCDAGYHMECLTPPldeVPIEEWFCPEC 46

PWWP_AtATX1-like

cd20142

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...

1450-1542

9.29e-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: 9.29e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1450 REIVWVKVGRYRWWPA-----EICHPRAVPSNIDKmrhDVGEFPVLFFGSNDYLWTHQARVFPYMEG---DVSSKDKMGK 1521
Cdd:cd20142      3 GDVVWAKVKGYPMWPAlvideEHAERCGLEANRPG---KKGTVPVQFFGTYEVARLNPKKVVGFSKGldlKYHSKCKAPV 79

                           90       100
                   ....*....|....*....|.
gi 1958702498 1522 gvdgtYKKALQEAAARFEELK 1542
Cdd:cd20142     80 -----FRQALEEAERYLKEGK 95

PHD_PHF21B

cd15524

PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) ...

1402-1441

9.46e-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: 39.11 E-value: 9.46e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1402 WCFVCSEGGSLLCCDSCPAAFHRECLNIDI---PEGNWYCNDC 1441
Cdd:cd15524      1 HCAACKRGGNLQPCGTCPRAYHLDCLDPPLktaPKGVWVCPKC 43

PHD_BS69

cd15537

PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing ...

1814-1854

9.93e-04

Pssm-ID: 277012 Cd Length: 43 Bit Score: 38.86 E-value: 9.93e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1814 CFSCGDGGQLVSCKkpGCPKVYHADCLNLTKRP--AGKWECPW 1854
Cdd:cd15537      2 CFECHAPGEVLPCS--GCFRVYHSDCLSEDFRPdsTSHWTCPV 42

PHD_PHF21A

cd15523

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...

1814-1853

1.12e-03

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 38.53 E-value: 1.12e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1814 CFSCGDGGQLVSCKKpgCPKVYHADCLN--LTKRPAGKWECP 1853
Cdd:cd15523      2 CSVCRKSGELLMCDT--CSLVYHLDCLDppLKTIPKGMWICP 41

PHD_ING

cd15505

PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a ...

1241-1279

1.14e-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: 38.82 E-value: 1.14e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1241 NCEKLGELLLCEAQCC--GAFHLECLGLTEMPRGKFICNEC 1279
Cdd:cd15505      5 NQVSYGEMVACDNPNCpiEWFHFECVGLTAKPKGKWYCPEC 45

PHD4_NSD2

cd15657

PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1814-1852

1.17e-03

Pssm-ID: 277127 Cd Length: 41 Bit Score: 38.45 E-value: 1.17e-03

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1814 CFSCGDGGQLVSCKKpgCPKVYHADCLNLtKRPAGKWEC 1852
Cdd:cd15657      2 CFVCSKGGSLLCCES--CPAAFHPDCLNI-EMPDGSWFC 37

SET_SMYD4

cd10536

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...

1711-1751

1.29e-03

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: 42.67 E-value: 1.29e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1711 FMNHCCQPNCETqkwSVNGDTrVGLFALSDIKAGTELTFNY 1751
Cdd:cd10536    153 LLNHSCDPNTIR---SFYGNT-IVVRATRPIKKGEEITICY 189

TNG2

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

1147-1280

1.33e-03

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

Pssm-ID: 227367 [Multi-domain] Cd Length: 271 Bit Score: 43.00 E-value: 1.33e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1147 KEFGGGTTRIFDKPRKRKRqrhGTARVHYKRVKKEDSARETPSSAEGELmIHRTAASPKEILEEGIEHDPGMSASKRLQG 1226
Cdd:COG5034    144 EHRSAASSQGSRHTKLKKR---KNIHNLKRRSPELSSKREVSFTLESPS-VPDTATRVKEGNNGGSTKSRGVSSEDNSEG 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958702498 1227 ERgggaalKENVCQNCEkLGELLLCEAQCCGA--FHLECLGLTEMPRGKFICNECR 1280
Cdd:COG5034    220 EE------LYCFCQQVS-YGQMVACDNANCKRewFHLECVGLKEPPKGKWYCPECK 268

PHD_BAZ1A_like

cd15544

PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...

1403-1441

1.34e-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: 38.55 E-value: 1.34e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVC---SEGGSLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15544      2 CKVCrkkGDPDNMILCDGCDKAFHLYCLRpalREVPSGDWFCPAC 46

PHA03307

transcriptional regulator ICP4; Provisional

1894-2268

1.40e-03

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 1.40e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1894 SCTEHDPC-GPNPLEPGEIREYVPPTATL-----------SPSPGTQQTEQSSEMGTQGPKKSDQPPTDATQMLSLSKKA 1961
Cdd:PHA03307    65 FEPPTGPPpGPGTEAPANESRSTPTWSLStlapasparegSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSP 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1962 VTGTCQRPLLPERPPERTDSSShlldriRDLAGSGTKSQSLVSSQRPQDRPPAKEGPRPQPPDRA-SPVTRPSSSPSVSS 2040
Cdd:PHA03307   145 GPPPAASPPAAGASPAAVASDA------ASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASpRPPRRSSPISASAS 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2041 LPLERPLRMTE-PRLDKSIGAASPKSQAV-----EKPPAPTGLRLSSPDRLLNTNSPKPQISDRPPDKSHASLTQRLPPP 2114
Cdd:PHA03307   219 SPAPAPGRSAAdDAGASSSDSSSSESSGCgwgpeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2115 EKVlsavvqslvakekalRPVDQNTQAKHRAAvvmdlidltprqKERAASPQEVTAQADEKTPVLESSSRPTSRGLGHVP 2194
Cdd:PHA03307   299 SPS---------------SPGSGPAPSSPRAS------------SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP 351

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958702498 2195 RaveKGGVSDPLQPPGKSAAPSEHPWQAVKSLTHARfLSPPSAKAFLYESAIQASGRAPVGSEQTPGPPSPAPG 2268
Cdd:PHA03307   352 S---PSRPPPPADPSSPRKRPRPSRAPSSPAASAGR-PTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGA 421

PHD_PHF21A

cd15523

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...

1238-1279

1.54e-03

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 38.15 E-value: 1.54e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1238 VCQNCEKLGELLLCEAqCCGAFHLECLG--LTEMPRGKFICNEC 1279
Cdd:cd15523      1 FCSVCRKSGELLMCDT-CSLVYHLDCLDppLKTIPKGMWICPKC 43

PHD5_NSD2

cd15660

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...

1403-1438

1.90e-03

Pssm-ID: 277130 Cd Length: 43 Bit Score: 37.99 E-value: 1.90e-03

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1403 CFVCSEGGSLLCCD--SCPAAFHRECLNI-DIPEGNWYC 1438
Cdd:cd15660      2 CFRCGDGGQLVLCDrkSCTKAYHLSCLGLtKRPFGKWEC 40

PWWP_ScIOC4-like

cd05840

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...

19-73

2.18e-03

Pssm-ID: 438965 Cd Length: 94 Bit Score: 39.59 E-value: 2.18e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958702498   19 GDLIWAKFKRRPWWPCRICSDPLI--NTHSKMKVANRRPYREYYVEAFGDPsEKAWV 73
Cdd:cd05840      1 GDLVLAKVKGYPPWPAMVLPEELLpkNVLKAKKRKPKSKKTVYPVQFFPDN-EYYWV 56

PHD_JADE3

cd15681

PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger ...

1403-1444

2.34e-03

PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (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. Jade-3 contains a canonical Cys4HisCys3 PHD domain followed by a non-canonical extended PHD (ePHD) domain, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.

Pssm-ID: 277151 [Multi-domain] Cd Length: 50 Bit Score: 38.03 E-value: 2.34e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1403 CFVC-----SEGGSLLCCDSCPAAFHRECLNI-DIPEGNWYCNDCKAG 1444
Cdd:cd15681      2 CDVCrspdsEEGNDMVFCDKCNICVHQACYGIlKVPEGSWLCRTCVLG 49

PHD_TIF1alpha

cd15622

PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also ...

1814-1852

2.53e-03

Pssm-ID: 277092 Cd Length: 43 Bit Score: 37.74 E-value: 2.53e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1814 CFSCGDGGQLVSCKKpgCPKVYHADCL--NLTKRPAGKWEC 1852
Cdd:cd15622      2 CAVCQNGGELLCCEK--CPKVFHLSCHvpTLMNFPSGEWIC 40

PWWP_NSD_rpt2

cd05838

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

18-37

2.53e-03

Pssm-ID: 438963 [Multi-domain] Cd Length: 96 Bit Score: 39.15 E-value: 2.53e-03

                           10        20
                   ....*....|....*....|
gi 1958702498   18 VGDLIWAKFKRRPWWPCRIC 37
Cdd:cd05838      2 YGDIVWVKLGNYRWWPAEIL 21

PHD3_NSD

cd15566

PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1403-1438

2.54e-03

Pssm-ID: 277041 Cd Length: 48 Bit Score: 37.79 E-value: 2.54e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1403 CFVCSEGGS-----LLCCDSCPAAFHRECLN---IDIPEGNWYC 1438
Cdd:cd15566      2 CATCEASGDgssgkLVRCIRCPRAYHAGCIPagsKLLNKKLIIC 45

PHD_BAZ2A

cd15629

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); BAZ2A, also ...

1403-1441

2.55e-03

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); 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. It contains 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.

Pssm-ID: 277099 Cd Length: 47 Bit Score: 37.91 E-value: 2.55e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEGGS---LLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15629      2 CLVCRKGDNdeyLLLCDGCDRGCHMYCHRpkmLQVPEGDWFCPNC 46

PWWP_PRKCBP1

cd20160

PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...

1445-1544

2.56e-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: 39.09 E-value: 2.56e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1445 KKPHyrEIVWVKVGRYRWWPAEIchpravpsnidkMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGD-VSSKDKMGKgv 1523
Cdd:cd20160      4 RKPH--LLVWAKLKGFPFWPAKA------------LRVNNGQVDVRFFGAHDRAWVPVKDCYLYSKEPpTSVKKKKSG-- 67

                           90       100
                   ....*....|....*....|.
gi 1958702498 1524 dgtYKKALQEAAARFEELKAQ 1544
Cdd:cd20160     68 ---LDEAMEELEIHIEKLREK 85

PHD_JADE

cd15573

PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family ...

1403-1441

2.58e-03

PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family includes proteins Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16), each of which is 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. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.

Pssm-ID: 277048 [Multi-domain] Cd Length: 46 Bit Score: 37.77 E-value: 2.58e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVC-----SEGGSLLCCDSCPAAFHRECLNI-DIPEGNWYCNDC 1441
Cdd:cd15573      2 CDVCrspdsEEGNEMVFCDKCNICVHQACYGIqKIPEGSWLCRTC 46

PHD2_CHD_II

cd15532

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1238-1279

2.86e-03

Pssm-ID: 277007 [Multi-domain] Cd Length: 43 Bit Score: 37.65 E-value: 2.86e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1238 VCQNCEKLGELLLCEaQCCGAFHLECLG--LTEMPRGKFICNEC 1279
Cdd:cd15532      1 FCRVCKDGGELLCCD-GCPSSYHLHCLNppLAEIPDGDWFCPRC 43

PHD5_NSD3

cd15661

PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

1239-1276

2.96e-03

Pssm-ID: 277131 Cd Length: 43 Bit Score: 37.64 E-value: 2.96e-03

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1239 CQNCEKLGELLLCEAQ-CCGAFHLECLGLTEMPRGKFIC 1276
Cdd:cd15661      2 CFQCGDGGELVMCDKKdCPKAYHLLCLNLTQPPYGKWEC 40

PHD_PRKCBP1

cd15538

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...

1239-1279

3.06e-03

Pssm-ID: 277013 Cd Length: 41 Bit Score: 37.31 E-value: 3.06e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1239 CQNCEKLGELLLCEaQCCGAFHLECLGLTEMPRGKFICNEC 1279
Cdd:cd15538      2 CWRCHKEGQVLCCS-LCPRVYHKKCLKLTSEPDEDWVCPEC 41

PHA03247

large tegument protein UL36; Provisional

1894-2252

3.12e-03

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 3.12e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1894 SCTEHDPCGPNPLEPGEIREYVPPTATLSP---SPGTQQTEQSSEMGTQGPKKSDQPPTDATQMLSLskkAVTGTCQRPL 1970
Cdd:PHA03247  2790 SLSESRESLPSPWDPADPPAAVLAPAAALPpaaSPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRP 2866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 1971 LPERPPERTDSSSHLldRIRDLAGSGTkSQSLVSSQRPQDRPPakegPRPQPPDRASPVTRPSSSPSVSSLPLERPLRMT 2050
Cdd:PHA03247  2867 PSRSPAAKPAAPARP--PVRRLARPAV-SRSTESFALPPDQPE----RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2051 EPRLDKSIGAAsPKSQAVEKPPAP-----TGLRLSSPDRLLNTNSPKPQISDRPPDKSHASLTQRlpppekvLSAVVQSL 2125
Cdd:PHA03247  2940 QPPLAPTTDPA-GAGEPSGAVPQPwlgalVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR-------VSSWASSL 3011

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2126 VAKEKALRPvdqntqakhraavvmdlidltPRQKERAASPQEVTAQADEKTPVLESSSRPTSRGLGHVPravekggvSDP 2205
Cdd:PHA03247  3012 ALHEETDPP---------------------PVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLP--------PEP 3062

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 2206 LQPPGKSAAPSEhPWQAVKSLTHARFLSPP-SAKAFLYESAIQASGRA 2252
Cdd:PHA03247  3063 HDPFAHEPDPAT-PEAGARESPSSQFGPPPlSANAALSRRYVRSTGRS 3109

PHD4_NSD1

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1239-1279

3.38e-03

Pssm-ID: 277126 Cd Length: 40 Bit Score: 37.30 E-value: 3.38e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1239 CQNCEKLGELLLCEAqCCGAFHLECLGLtEMPRGKFICNEC 1279
Cdd:cd15656      2 CFVCSEGGSLLCCES-CPAAFHRECLNI-DMPEGSWYCNDC 40

PHD_TAF3

cd15522

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...

1402-1441

3.42e-03

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53).

Pssm-ID: 276997 [Multi-domain] Cd Length: 46 Bit Score: 37.27 E-value: 3.42e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958702498 1402 WCFVCS---EGGSLLCCDSCPAAFHRECLNIDIP---EGNWYCNDC 1441
Cdd:cd15522      1 ICPICKkpdDGSPMIGCDECDDWYHWECVGITDEppeEDDWFCPKC 46

PHD_ING3

cd15585

PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also ...

1246-1279

3.88e-03

Pssm-ID: 277060 [Multi-domain] Cd Length: 45 Bit Score: 37.05 E-value: 3.88e-03

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958702498 1246 GELLLCEAQCCGA--FHLECLGLTEMPRGKFICNEC 1279
Cdd:cd15585     10 GEMVGCDNDDCPIewFHYGCVGLTEAPKGKWYCPQC 45

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1814-1860

3.90e-03

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 37.47 E-value: 3.90e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958702498 1814 CFSCGDGGQLVSCKkpGCPKVYHADCLNLTKRPA----GKWECPwhQCDVC 1860
Cdd:pfam00628    5 CGKSDDGGELVQCD--GCDDWFHLACLGPPLDPAeipsGEWLCP--ECKPK 51

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1285-1331

3.91e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 37.19 E-value: 3.91e-03

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1958702498  1285 TCFVCKQSGEDVK--RCLLplCGKFYHEECVQKYPPTVVQNKGFRCPLH 1331
Cdd:smart00249    1 YCSVCGKPDDGGEllQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

PHD4_NSD1

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...

1814-1852

4.03e-03

Pssm-ID: 277126 Cd Length: 40 Bit Score: 36.92 E-value: 4.03e-03

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958702498 1814 CFSCGDGGQLVSCKKpgCPKVYHADCLNLtKRPAGKWEC 1852
Cdd:cd15656      2 CFVCSEGGSLLCCES--CPAAFHRECLNI-DMPEGSWYC 37

PHD2_NSD

cd15565

PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

1813-1855

4.24e-03

Pssm-ID: 277040 Cd Length: 51 Bit Score: 37.41 E-value: 4.24e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958702498 1813 ECFSCG----DGGQLVSCKKPGCPKVYHADCL----NLTKRPAGKWECPWH 1855
Cdd:cd15565      1 SCFVCKklgsVGGEVFKCSVASCGKFYHEECLkkwpLTTISDSKKFRCPLH 51

PHD1_Lid2p_like

cd15519

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...

1814-1853

4.39e-03

Pssm-ID: 276994 [Multi-domain] Cd Length: 46 Bit Score: 37.06 E-value: 4.39e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1814 CFSCG---DGGQLVSCKkpGCPKVYHADCLN--LTKRPAGKWECP 1853
Cdd:cd15519      2 CEVCGlddNEGEVLLCD--GCDAEYHTSCLDppLGEIPPGTWFCP 44

PHD1_CHD_II

cd15531

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1239-1279

4.52e-03

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 37.20 E-value: 4.52e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958702498 1239 CQNCEKLGELLLCEAqCCGAFHLECLG--LTEMPRGKFICNEC 1279
Cdd:cd15531      2 CEVCQQGGEIILCDT-CPRAYHLVCLDpeLEKAPEGKWSCPHC 43

PHD1_KMT2A_like

cd15506

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

1403-1441

4.99e-03

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation through mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger.

Pssm-ID: 276981 Cd Length: 47 Bit Score: 36.95 E-value: 4.99e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958702498 1403 CFVCSEGG--SLLCCDSCPAAFHRECLN-----IDIPEGNWYCNDC 1441
Cdd:cd15506      2 CFLCGSAGlnELLYCSVCCEPYHTFCLEeaerpLNINKDNWCCRRC 47

PHA03247

large tegument protein UL36; Provisional

2006-2267

5.08e-03

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 5.08e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2006 QRP-QDRPPAKEGPRPQP-----PDRASPVTrpssspsvsslplerPLRMTEPRL-DKSIGAASPKS-----QAVEK--- 2070
Cdd:PHA03247  2481 RRPaEARFPFAAGAAPDPggggpPDPDAPPA---------------PSRLAPAILpDEPVGEPVHPRmltwiRGLEElas 2545

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2071 -------PPAPTGLRLSSPDRLLNTNSPKPQISD--------RP--PDKSHASLTQRLPPPEKVLSAVVQSLVAKEKALR 2133
Cdd:PHA03247  2546 ddagdppPPLPPAAPPAAPDRSVPPPRPAPRPSEpavtsrarRPdaPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958702498 2134 -PVDQNTQAKHRAAVVMDLIDLTPRQKERAASPQEVTAQadEKTPVLESSSRPTSRGLGHVPRAVEK-----GGVSDPlQ 2207
Cdd:PHA03247  2626 pPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP--RRARRLGRAAQASSPPQRPRRRAARPtvgslTSLADP-P 2702

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958702498 2208 PPGKSAAPSEHPWQAVKSLT----HARFLSP-----PSAKAFLYESAIQASGRAPVGSEQTPGPPSPAP 2267
Cdd:PHA03247  2703 PPPPTPEPAPHALVSATPLPpgpaAARQASPalpaaPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP 2771

PHD1_NSD1_2

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...

1403-1442

5.40e-03

Pssm-ID: 277118 Cd Length: 43 Bit Score: 36.68 E-value: 5.40e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCD-SCPAAFHRECLNI-DIPEGNWYCNDCK 1442
Cdd:cd15648      2 CQVCEKPGELLLCEgQCCGAFHLDCIGLsEMPSGKFICDECI 43

PHD2_PHF10

cd15529

PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...

1246-1279

5.57e-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: 36.90 E-value: 5.57e-03

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958702498 1246 GELLLCEaQCCGAFHLECLGLTEMPRGKFICNEC 1279
Cdd:cd15529     12 DKMMFCD-QCDRGYHTFCVGLRSIPDGRWICPLC 44

PHD_TIF1delta

cd15625

PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta); TIF1delta, also ...

1811-1852

5.59e-03

Pssm-ID: 277095 [Multi-domain] Cd Length: 49 Bit Score: 36.86 E-value: 5.59e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958702498 1811 EDECFSCGDGGQLVSCKKpgCPKVYHADCL--NLTKRPAGKWEC 1852
Cdd:cd15625      2 EDFCAVCLNGGELLCCDR--CPKVFHLSCHvpALLSFPVGEWVC 43

PHD_ING2

cd15683

PHD finger found in inhibitor of growth protein 2 (ING2); ING2, also termed inhibitor of ...

1821-1853

5.85e-03

PHD finger found in inhibitor of growth protein 2 (ING2); ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. ING2 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.

Pssm-ID: 277153 [Multi-domain] Cd Length: 49 Bit Score: 36.92 E-value: 5.85e-03

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958702498 1821 GQLVSCKKPGCP-KVYHADCLNLTKRPAGKWECP 1853
Cdd:cd15683     11 GEMIGCDNEQCPiEWFHFSCVGLTYKPKGKWYCP 44

PHD_TIF1beta

cd15623

PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also ...

1403-1441

6.04e-03

PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also termed Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), or KRAB-interacting protein 1 (KRIP-1), or nuclear co-repressor KAP-1, or RING finger protein 96, or tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, acts as a nuclear co-repressor that plays a role in transcription and in DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. In addition, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. TIF1-beta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), which can interact with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and mediates homo- and heterodimerization, a plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region, which interact with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity.

Pssm-ID: 277093 Cd Length: 43 Bit Score: 36.71 E-value: 6.04e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHREC---LNIDIPEGNWYCNDC 1441
Cdd:cd15623      2 CRVCQKAGALVMCDQCEFCFHLDChlpALQEVPGEDWKCLLC 43

PHD1_Lid_like

cd15605

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...

1403-1441

6.27e-03

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar proteins; Drosophila melanogaster Lid, also termed Retinoblastoma-binding protein 2 homolog, is identified genetically as a trithorax group (trxG) protein that is a Drosophila homolog of the human protein JARID1A/kdm5A, a member of the JARID subfamily within the JmjC proteins. Lid functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Lid contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger of Lid.

Pssm-ID: 277078 Cd Length: 46 Bit Score: 36.66 E-value: 6.27e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEGG---SLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15605      2 CHTCGRGDgeeSMLLCDGCDDSYHTFCLLpplSEVPKGDWRCPKC 46

PHD2_PHF12_Rco1

cd15534

PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...

1814-1855

6.44e-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: 36.56 E-value: 6.44e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958702498 1814 CFSC---GDGGQLVSCKKpgCPKVYHADCLN--LTKRPA-GKWECPWH 1855
Cdd:cd15534      2 CFKCnrsCRVAPLIQCDY--CPLLFHLDCLDppLTHPPAtGRWMCPNH 47

TNG2

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

1402-1442

7.11e-03

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

Pssm-ID: 227367 [Multi-domain] Cd Length: 271 Bit Score: 40.69 E-value: 7.11e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1402 WCFvCSEG--GSLLCCDS--CPAA-FHRECLNI-DIPEGNWYCNDCK 1442
Cdd:COG5034    223 YCF-CQQVsyGQMVACDNanCKREwFHLECVGLkEPPKGKWYCPECK 268

ADDz_ATRX

cd11726

ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...

1406-1427

7.12e-03

ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a PHD-like zinc finger domain of ATRX, which belongs to the SNF2 family of chromatin remodeling proteins. ATRX is a large chromatin-associated nuclear protein with two domains, ADDz_ATRX at the N-terminus, followed by a C-terminal ATPase/helicase domain. The ADDz_ATRX domain recognizes a specific methylated histone, and this interaction is required for heterochromatin localization of the ATRX protein. Missense mutations in either of the two ATRX domains lead to the X-linked alpha-thalassemia and mental retardation syndrome; however the mutations in the ADDz_ATRX domain produce a more severe disease phenotype that may also relate to disturbing unknown functions or interaction sites of this domain. The ADDz domain is also present in chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3); it 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: 277252 [Multi-domain] Cd Length: 102 Bit Score: 38.06 E-value: 7.12e-03

                           10        20
                   ....*....|....*....|..
gi 1958702498 1406 CSEGGSLLCCDSCPAAFHRECL 1427
Cdd:cd11726     56 CGQGGDLICCDFCPNVFCKKCI 77

PHD_ING1_2

cd15584

PHD finger found in inhibitor of growth protein 1 (ING1) and 2 (ING2); ING1 is an epigenetic ...

1821-1853

7.54e-03

PHD finger found in inhibitor of growth protein 1 (ING1) and 2 (ING2); 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 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 and phosphorylate ING1 and further regulates its activity. ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, belongs to the inhibitor of growth (ING) family of type II tumor suppressors. It is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. Both ING1 and ING2 contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.

Pssm-ID: 277059 [Multi-domain] Cd Length: 45 Bit Score: 36.27 E-value: 7.54e-03

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958702498 1821 GQLVSCKKPGCP-KVYHADCLNLTKRPAGKWECP 1853
Cdd:cd15584     10 GEMIGCDNDECPiEWFHFSCVGLTHKPKGKWYCP 43

PHD1_KDM5A_like

cd15515

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...

1403-1441

7.71e-03

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar proteins; The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me2 and H3K4me3), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. This family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent H3K4me3 demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 276990 Cd Length: 46 Bit Score: 36.60 E-value: 7.71e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEGG---SLLCCDSCPAAFHRECLN---IDIPEGNWYCNDC 1441
Cdd:cd15515      2 CQVCGRGDdedKLLLCDGCDDSYHTFCLIpplPDIPPGDWRCPKC 46

PHD_SP110_140

cd15626

PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family ...

1403-1441

7.77e-03

PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family includes nuclear body proteins SP100, SP140, and similar proteins. Sp110, also termed interferon-induced protein 41/75, or speckled 110 kDa, or transcriptional coactivator 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. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population. Sp110 contains a Sp100-like domain, a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD). SP140, also termed lymphoid-restricted homolog of Sp100 (LYSp100), or nuclear autoantigen Sp-140, or speckled 140 kDa, 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's viral infectivity factor (Vif) protein. Sp140 contains a nuclear localization signal, a dimerization domain (HSR or CARD domain), a SAND domain, a PHD finger, and a BRD.

Pssm-ID: 277096 Cd Length: 42 Bit Score: 36.25 E-value: 7.77e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958702498 1403 CFVCSEGGSLLCCDSCPAAFHRECL--NIDIPEGNWYCNDC 1441
Cdd:cd15626      2 CEVCGQEGKLFCCCTCSRVFHEDCHipPVEAQRSPWSCTFC 42

COG5141

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

1403-1445

7.83e-03

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

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 41.51 E-value: 7.83e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958702498 1403 CFVCSEGGS-----LLCCDSCPAAFHRECLNI-DIPEGNWYCNDCKAGK 1445
Cdd:COG5141    196 CTKCTSTHNensnaIVFCDGCEICVHQSCYGIqFLPEGFWLCRKCIYGE 244

PHD_ING

cd15505

PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a ...

1821-1853

8.19e-03

Pssm-ID: 276980 [Multi-domain] Cd Length: 45 Bit Score: 36.12 E-value: 8.19e-03

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958702498 1821 GQLVSCKKPGCP-KVYHADCLNLTKRPAGKWECP 1853
Cdd:cd15505     10 GEMVACDNPNCPiEWFHFECVGLTAKPKGKWYCP 43

PHD1_Rco1

cd15535

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...

1814-1860

8.23e-03

Pssm-ID: 277010 [Multi-domain] Cd Length: 45 Bit Score: 36.24 E-value: 8.23e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958702498 1814 CFSCGDGGQLVSCKkpGCPKVYHADCLNLTKRPAGKWECPWHqCDVC 1860
Cdd:cd15535      2 CSACGGYGSFLCCD--GCPRSFHFSCLDPPLEEDNLPDDEWF-CNEC 45

PHD_BRPF1

cd15676

PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar ...

1403-1441

8.62e-03

PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins; BRPF1, also termed peregrin or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ)-dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains 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. BRPF1 may be involved in chromatin remodeling. This model corresponds to the canonical Cys4HisCys3 PHD finger.

Pssm-ID: 277146 [Multi-domain] Cd Length: 62 Bit Score: 36.96 E-value: 8.62e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958702498 1403 CFVCSEG-----GSLLCCDSCPAAFHRECLNID-IPEGNWYCNDC 1441
Cdd:cd15676     10 CCICNDGecqnsNVILFCDMCNLAVHQECYGVPyIPEGQWLCRRC 54

TNG2