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Conserved domains on  [gi|17136558|ref|NP_476770|]
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trithorax, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 3207-3358 3.94e-111

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: 350.15  E-value: 3.94e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3207 MAMKYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDA 3286
Cdd:cd19170    1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136558 3287 TMRGNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCRKYLN 3358
Cdd:cd19170   81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDVKIPCTCGSKKCRKYLN 152
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 1369-1473 2.50e-66

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of 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 by 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 PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


:

Pssm-ID: 277134  Cd Length: 105  Bit Score: 219.97  E-value: 2.50e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGE 1448
Cdd:cd15664    1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                         90       100
                 ....*....|....*....|....*
gi 17136558 1449 HYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15664   81 NYHFMCARKAECVFQDDKKVFCPAH 105
PHD3_KMT2A_like cd15508
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 1055-1111 5.31e-34

PHD finger 3 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 third PHD finger.


:

Pssm-ID: 276983  Cd Length: 57  Bit Score: 125.64  E-value: 5.31e-34
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCPICQRCYDDNDFDLKMMECGDCGQWVHSKCEGLSDEQYNLLSTLPESIEFICKKC 1111
Cdd:cd15508    1 YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC 57
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 3020-3108 6.95e-28

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region (FYRN), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.


:

Pssm-ID: 197781  Cd Length: 86  Bit Score: 109.31  E-value: 6.95e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558    3020 HLLYEIQSEDGFTYKSSSITEIWEKVFEAVQVARRAHGLtplPEGPLADMGGIQMIGLKTNALKYLIEQLPGVEKCSKYT 3099
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADL---LQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYW 77


                    ....*....
gi 17136558    3100 PKYHKRNGN 3108
Cdd:smart00542   78 FRYHRSPLL 86
PHD1_KMT2A_like cd15506
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 900-976 2.26e-12

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: 63.92  E-value: 2.26e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558  900 LCFLCGSTGLDPLIFCACCCEPYHQYCVQDEynlkhgsfedttlmgsllETTVNASTGpssslnqltqrlNWLCPRC 976
Cdd:cd15506    1 LCFLCGSAGLNELLYCSVCCEPYHTFCLEEA------------------ERPLNINKD------------NWCCRRC 47
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 1522-1569 1.48e-09

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.


:

Pssm-ID: 461787  Cd Length: 51  Bit Score: 55.97  E-value: 1.48e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 17136558   1522 GSLEVRQLGAIVPRFSDSY--EAVVPINFLCSRLYWSSKEPWKIVEYTVR 1569
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPAFHteRYIYPVGYKSTRLYWSTKDPRKRCRYTCE 50
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 978-1022 1.66e-05

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: 44.51  E-value: 1.66e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 17136558     978 VCYTCNMS--SGSKVKCQKCQKNYHSTCLGTSKRLLGADRPLICVNC 1022
Cdd:smart00249    1 YCSVCGKPddGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PRK13914 super family cl36314
invasion associated endopeptidase;
638-856 2.39e-05

invasion associated endopeptidase;


The actual alignment was detected with superfamily member PRK13914:

Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 49.80  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   638 TQAGTKKSGAAEAQVEEVQPQKEEAPQTSTTTQPSASNGASHGVPQAELAGE-----TNAT------GDTLKRQRIDLkG 706
Cdd:PRK13914  140 TDKVTSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAETKEtpvvdQNATthavksGDTIWALSVKY-G 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   707 PRVKHV-----CRSASIVLGQPLATfgedQQPEDAADMQQEIAAPVPSAimepspEKPTHIVTDENDNCASCKTspvgdE 781
Cdd:PRK13914  219 VSVQDImswnnLSSSSIYVGQKLAI----KQTANTATPKAEVKTEAPAA------EKQAAPVVKENTNTNTATT-----E 283

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136558   782 SKpsKSSGSAQAEVKKATALGKEGTASAAGGSSAKVTTRNAAVASNLIVAASKKQRNGDIATSSSVTQSSNQTQG 856
Cdd:PRK13914  284 KK--ETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQG 356
NR_DBD_like super family cl02596
DNA-binding domain of nuclear receptors is composed of two C4-type zinc fingers; DNA-binding ...
 394-488 4.47e-05

DNA-binding domain of nuclear receptors is composed of two C4-type zinc fingers; DNA-binding domain of nuclear receptors is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. It interacts with a specific DNA site upstream of the target gene and modulates the rate of transcriptional initiation. Nuclear receptors form a superfamily of ligand-activated transcription regulators, which regulate various physiological functions, from development, reproduction, to homeostasis and metabolism in animals (metazoans). The family contains not only receptors for known ligands but also orphan receptors for which ligands do not exist or have not been identified. NRs share a common structural organization with a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). Most nuclear receptors bind as homodimers or heterodimers to their target sites, which consist of two hexameric half-sites. Specificity is determined by the half-site sequence, the relative orientation of the half-sites and the number of spacer nucleotides between the half-sites. However, a growing number of nuclear receptors have been reported to bind to DNA as monomers.


The actual alignment was detected with superfamily member cd07163:

Pssm-ID: 413390  Cd Length: 92  Bit Score: 44.79  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558  394 CSICSAVVSSKEvtqarkYGVVACDVCRKFFskmtKKSISANsstantssgsQQYLqCKGNEGSPCSIhsaksqlknfKK 473
Cdd:cd07163    9 CKVCGDRSSGKH------YGIYACDGCSGFF----KRSIRRN----------RQYV-CKSKGQGGCPV----------DK 57

                         90
                 ....*....|....*
gi 17136558  474 FYKDRCTACWLKKCM 488
Cdd:cd07163   58 THRNQCRACRLKKCF 72
 
Name Accession Description Interval E-value
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 3207-3358 3.94e-111

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: 350.15  E-value: 3.94e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3207 MAMKYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDA 3286
Cdd:cd19170    1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136558 3287 TMRGNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCRKYLN 3358
Cdd:cd19170   81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDVKIPCTCGSKKCRKYLN 152
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 1369-1473 2.50e-66

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of 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 by 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 PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277134  Cd Length: 105  Bit Score: 219.97  E-value: 2.50e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGE 1448
Cdd:cd15664    1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                         90       100
                 ....*....|....*....|....*
gi 17136558 1449 HYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15664   81 NYHFMCARKAECVFQDDKKVFCPAH 105
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 3222-3342 1.01e-44

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 159.04  E-value: 1.01e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558    3222 VGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGI-GCYMFKIDDNLVVDATMRGNAARFINHCC 3300
Cdd:smart00317    3 LEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHSC 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 17136558    3301 EPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDE 3342
Cdd:smart00317   83 EPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
3226-3355 2.64e-38

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 140.87  E-value: 2.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3226 RSHIHGRGLYCTKDIEAGEMVIEYAGELIrsTLTDKRERYYDSRGIGCYMFKIDDNLVVDATMRGNAARFINHCCEPNCY 3305
Cdd:COG2940   12 PSPIHGRGVFATRDIPKGTLIGEYPGEVI--TWAEAERREPHKEPLHTYLFELDDDGVIDGALGGNPARFINHSCDPNCE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17136558 3306 SKVVDilghKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCgsKRCRK 3355
Cdd:COG2940   90 ADEED----GRIFIVALRDIAAGEELTYDYGLDYDEEEYPCRC--PNCRG 133
PHD3_KMT2A_like cd15508
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 1055-1111 5.31e-34

PHD finger 3 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 third PHD finger.


Pssm-ID: 276983  Cd Length: 57  Bit Score: 125.64  E-value: 5.31e-34
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCPICQRCYDDNDFDLKMMECGDCGQWVHSKCEGLSDEQYNLLSTLPESIEFICKKC 1111
Cdd:cd15508    1 YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC 57
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 3231-3336 9.30e-32

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: 121.48  E-value: 9.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   3231 GRGLYCTKDIEAGEMVIEYAGE-LIRSTLTDKRERYY----DSRGIGCYMFKIDDN--LVVDAT--MRGNAARFINHCCE 3301
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYydklELRLWGPYLFTLDEDseYCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 17136558   3302 PNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYK 3336
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 3020-3108 6.95e-28

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region (FYRN), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.


Pssm-ID: 197781  Cd Length: 86  Bit Score: 109.31  E-value: 6.95e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558    3020 HLLYEIQSEDGFTYKSSSITEIWEKVFEAVQVARRAHGLtplPEGPLADMGGIQMIGLKTNALKYLIEQLPGVEKCSKYT 3099
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADL---LQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYW 77


                    ....*....
gi 17136558    3100 PKYHKRNGN 3108
Cdd:smart00542   78 FRYHRSPLL 86
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 3018-3103 1.73e-23

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.


Pssm-ID: 461788  Cd Length: 83  Bit Score: 96.52  E-value: 1.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   3018 GPHLLYEIQSEDGFTYKSSSITEIWEKVFEAVQVARRAHGLTPlpeGPLADMGGIQMIGLKTNALKYLIEQLPGVEKCSK 3097
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKL---KLPESISGEDMFGLTHPAVVRLIESLPGAEKCTN 77


                   ....*.
gi 17136558   3098 YTPKYH 3103
Cdd:pfam05965   78 YKFRYG 83
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 1396-1473 1.86e-13

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 68.12  E-value: 1.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   1396 HTNCAMWSAEV-FEEIDG---SLQNVHSAVARGRMIKCTVCGNR-GATVGCNVRSCGEHYHYPCARSIDCAFLTDKS--- 1467
Cdd:pfam13771    1 HVVCALWSPELvQRGNDSmgfPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDEDngt 80


                   ....*...
gi 17136558   1468 --MYCPAH 1473
Cdd:pfam13771   81 fkSYCKKH 88
PHD1_KMT2A_like cd15506
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 900-976 2.26e-12

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: 63.92  E-value: 2.26e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558  900 LCFLCGSTGLDPLIFCACCCEPYHQYCVQDEynlkhgsfedttlmgsllETTVNASTGpssslnqltqrlNWLCPRC 976
Cdd:cd15506    1 LCFLCGSAGLNELLYCSVCCEPYHTFCLEEA------------------ERPLNINKD------------NWCCRRC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1055-1114 6.16e-10

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: 57.12  E-value: 6.16e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   1055 FCPICQRCYDDNDfdlkMMECGDCGQWVHSKCEGLSDEQYNLLSTlpesiEFICKKCARR 1114
Cdd:pfam00628    1 YCAVCGKSDDGGE----LVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPECKPK 51
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 1522-1569 1.48e-09

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.


Pssm-ID: 461787  Cd Length: 51  Bit Score: 55.97  E-value: 1.48e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 17136558   1522 GSLEVRQLGAIVPRFSDSY--EAVVPINFLCSRLYWSSKEPWKIVEYTVR 1569
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPAFHteRYIYPVGYKSTRLYWSTKDPRKRCRYTCE 50
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
 1529-1574 1.24e-08

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region (FYRC), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.


Pssm-ID: 128814  Cd Length: 44  Bit Score: 53.06  E-value: 1.24e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 17136558    1529 LGAIVPRFSDSYEAVVPINFLCSRLYWSSKEPWKIVEYtvRTTIQN 1574
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLY--SCVIDE 44
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1055-1111 3.66e-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: 51.83  E-value: 3.66e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558    1055 FCPICQRCYDDNDfdlkMMECGDCGQWVHSKCEGLSDEQYNLLStlpesiEFICKKC 1111
Cdd:smart00249    1 YCSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLLEEEPDG------KWYCPKC 47
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 978-1022 1.66e-05

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: 44.51  E-value: 1.66e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 17136558     978 VCYTCNMS--SGSKVKCQKCQKNYHSTCLGTSKRLLGADRPLICVNC 1022
Cdd:smart00249    1 YCSVCGKPddGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PRK13914 PRK13914
invasion associated endopeptidase;
638-856 2.39e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 49.80  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   638 TQAGTKKSGAAEAQVEEVQPQKEEAPQTSTTTQPSASNGASHGVPQAELAGE-----TNAT------GDTLKRQRIDLkG 706
Cdd:PRK13914  140 TDKVTSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAETKEtpvvdQNATthavksGDTIWALSVKY-G 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   707 PRVKHV-----CRSASIVLGQPLATfgedQQPEDAADMQQEIAAPVPSAimepspEKPTHIVTDENDNCASCKTspvgdE 781
Cdd:PRK13914  219 VSVQDImswnnLSSSSIYVGQKLAI----KQTANTATPKAEVKTEAPAA------EKQAAPVVKENTNTNTATT-----E 283

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136558   782 SKpsKSSGSAQAEVKKATALGKEGTASAAGGSSAKVTTRNAAVASNLIVAASKKQRNGDIATSSSVTQSSNQTQG 856
Cdd:PRK13914  284 KK--ETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQG 356
NR_DBD_TLX cd07163
DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers; DNA-binding ...
 394-488 4.47e-05

DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers; DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. TLX interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. TLX is an orphan receptor that is expressed by neural stem/progenitor cells in the adult brain of the subventricular zone (SVZ) and the dentate gyrus (DG). It plays a key role in neural development by promoting cell cycle progression and preventing apoptosis in the developing brain. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TLX has a central well conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 143537  Cd Length: 92  Bit Score: 44.79  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558  394 CSICSAVVSSKEvtqarkYGVVACDVCRKFFskmtKKSISANsstantssgsQQYLqCKGNEGSPCSIhsaksqlknfKK 473
Cdd:cd07163    9 CKVCGDRSSGKH------YGIYACDGCSGFF----KRSIRRN----------RQYV-CKSKGQGGCPV----------DK 57

                         90
                 ....*....|....*
gi 17136558  474 FYKDRCTACWLKKCM 488
Cdd:cd07163   58 THRNQCRACRLKKCF 72
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1429-1473 8.41e-05

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: 42.58  E-value: 8.41e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 17136558    1429 CTVCG---NRGATVGCNvrSCGEHYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:smart00249    2 CSVCGkpdDGGELLQCD--GCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 975-1022 2.61e-04

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 41.15  E-value: 2.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 17136558  975 RCTVCYTCNMSSGSKVKCQKCQKNYHSTCLGTSKRLLGADRPLICVNC 1022
Cdd:cd15489    1 SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 901-976 4.02e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 40.66  E-value: 4.02e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558     901 CFLCGST-GLDPLIFCACCCEPYHQYCVQDEYNLKhgsfedttlmgsllettvnastgpssslnqlTQRLNWLCPRC 976
Cdd:smart00249    2 CSVCGKPdDGGELLQCDGCDRWYHQTCLGPPLLEE-------------------------------EPDGKWYCPKC 47
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
1394-1512 1.24e-03

PHD zinc finger-containing protein [General function prediction only];


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 44.59  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1394 WVHTNCAMWSAEVF-------EEIDGsLQNVHSAVARgrmIKCTVCGNRGAT-VGCNVRSCGEHYHYPCARSiDCAFLT- 1464
Cdd:COG5141  268 WGHVICAMFNPELSfghllskDPIDN-IASVSSSRWK---LGCLICKEFGGTcIQCSYFNCTRAYHVTCARR-AGYFDLn 342

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136558 1465 -----------DKSMYCPAHAK----NGNALKANGSPSVtYESNFEVSRPVYVELDRKRKKLI 1512
Cdd:COG5141  343 iyshngisyciDHEPLCRKHYPlgygRMNGLRYFGYEKL-RYKNPPTAIPRKVRAARPRATLF 404
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 901-979 1.57e-03

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 39.01  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558    901 CFLCGSTGLD-PLIFCACCCEPYHQYCVQ---DEYNLKHGsfedttlmgsllettvnastgpssslnqltqrlNWLCPRC 976
Cdd:pfam00628    2 CAVCGKSDDGgELVQCDGCDDWFHLACLGpplDPAEIPSG---------------------------------EWLCPEC 48


                   ...
gi 17136558    977 TVC 979
Cdd:pfam00628   49 KPK 51
 
Name Accession Description Interval E-value
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 3207-3358 3.94e-111

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: 350.15  E-value: 3.94e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3207 MAMKYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDA 3286
Cdd:cd19170    1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136558 3287 TMRGNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCRKYLN 3358
Cdd:cd19170   81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDVKIPCTCGSKKCRKYLN 152
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 3207-3354 3.63e-83

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: 269.85  E-value: 3.63e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3207 MAMKYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGI-GCYMFKIDDNLVVD 3285
Cdd:cd10518    1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGgGTYMFRIDEDLVID 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3286 ATMRGNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFED-EKIPCSCGSKRCR 3354
Cdd:cd10518   81 ATKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDeEKIPCLCGAPNCR 150
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 3207-3358 3.90e-82

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: 267.27  E-value: 3.90e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3207 MAMKYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDA 3286
Cdd:cd19206    1 MPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136558 3287 TMRGNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFED--EKIPCSCGSKRCRKYLN 3358
Cdd:cd19206   81 TMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDasNKLPCNCGAKKCRKFLN 154
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 3207-3358 9.09e-75

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: 246.09  E-value: 9.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3207 MAMKYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDA 3286
Cdd:cd19207    1 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136558 3287 TMRGNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFED--EKIPCSCGSKRCRKYLN 3358
Cdd:cd19207   81 TMHGNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDasNKLPCNCGAKRCRRFLN 154
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 1369-1473 2.50e-66

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of 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 by 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 PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277134  Cd Length: 105  Bit Score: 219.97  E-value: 2.50e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGE 1448
Cdd:cd15664    1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                         90       100
                 ....*....|....*....|....*
gi 17136558 1449 HYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15664   81 NYHFMCARKAECVFQDDKKVFCPAH 105
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 3226-3354 7.69e-64

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: 214.51  E-value: 7.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3226 RSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIG-CYMFKIDDNLVVDATMRGNAARFINHCCEPNC 3304
Cdd:cd19169   19 KSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGsSYLFRVDDDTIIDATKCGNLARFINHSCNPNC 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17136558 3305 YSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCR 3354
Cdd:cd19169   99 YAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDEKIPCLCGAPQCR 148
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 3210-3357 2.28e-62

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: 210.36  E-value: 2.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3210 KYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDATMR 3289
Cdd:cd19171    4 QYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDATMT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3290 GNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDE--KIPCSCGSKRCRKYL 3357
Cdd:cd19171   84 GGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDqhKIPCLCGAPNCRKWM 153
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 3226-3354 7.48e-59

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: 200.34  E-value: 7.48e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3226 RSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIG-CYMFKIDDNLVVDATMRGNAARFINHCCEPNC 3304
Cdd:cd20072   19 RSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDATKKGNIARFINHCCDPNC 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17136558 3305 YSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCR 3354
Cdd:cd20072   99 TAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREEDKIPCLCGAPNCR 148
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 3226-3358 9.92e-48

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: 168.66  E-value: 9.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3226 RSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGC-YMFKIDDNLVVDATMRGNAARFINHCCEPNC 3304
Cdd:cd19204   20 RSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLARFINHCCTPNC 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17136558 3305 YSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCRKYLN 3358
Cdd:cd19204  100 YAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIEDNKIPCLCGTENCRGTLN 153
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
 3210-3357 2.53e-46

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: 164.80  E-value: 2.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3210 KYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDATMR 3289
Cdd:cd19208    5 QYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVIDATLT 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3290 GNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDE--KIPCSCGSKRCRKYL 3357
Cdd:cd19208   85 GGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWM 154
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 3209-3358 2.89e-45

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: 161.76  E-value: 2.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3209 MKYRTLKeTYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGC-YMFKIDDNLVVDAT 3287
Cdd:cd19205    4 LKFNQLK-FRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDAT 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136558 3288 MRGNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCRKYLN 3358
Cdd:cd19205   83 KCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIPCLCGSENCRGTLN 153
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 3222-3342 1.01e-44

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 159.04  E-value: 1.01e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558    3222 VGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGI-GCYMFKIDDNLVVDATMRGNAARFINHCC 3300
Cdd:smart00317    3 LEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHSC 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 17136558    3301 EPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDE 3342
Cdd:smart00317   83 EPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 3210-3357 1.11e-44

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: 159.86  E-value: 1.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3210 KYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDATMR 3289
Cdd:cd19209    6 QYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLT 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3290 GNAARFINHCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEK--IPCSCGSKRCRKYL 3357
Cdd:cd19209   86 GGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQhkIPCHCGAWNCRKWM 155
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 1367-1473 6.06e-40

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2A. KMT2A also termed ALL-1, or CXXC-type zinc finger protein 7, or myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), or trithorax-like protein (Htrx), or zinc finger protein HRX, is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It 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, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, a Bromodomain domain, this extended PHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277163  Cd Length: 113  Bit Score: 144.76  E-value: 6.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1367 RMCLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSC 1446
Cdd:cd15693    1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                         90       100
                 ....*....|....*....|....*..
gi 17136558 1447 GEHYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15693   81 TSNYHFMCSRAKNCVFLEDKKVYCQRH 107
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1369-1473 2.54e-39

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C, and KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.


Pssm-ID: 277136  Cd Length: 105  Bit Score: 142.83  E-value: 2.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGE 1448
Cdd:cd15666    1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                         90       100
                 ....*....|....*....|....*
gi 17136558 1449 HYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15666   81 VYHLPCAIKDGCMFFKDKTMLCPSH 105
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
3226-3355 2.64e-38

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 140.87  E-value: 2.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3226 RSHIHGRGLYCTKDIEAGEMVIEYAGELIrsTLTDKRERYYDSRGIGCYMFKIDDNLVVDATMRGNAARFINHCCEPNCY 3305
Cdd:COG2940   12 PSPIHGRGVFATRDIPKGTLIGEYPGEVI--TWAEAERREPHKEPLHTYLFELDDDGVIDGALGGNPARFINHSCDPNCE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17136558 3306 SKVVDilghKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCgsKRCRK 3355
Cdd:COG2940   90 ADEED----GRIFIVALRDIAAGEELTYDYGLDYDEEEYPCRC--PNCRG 133
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 3222-3354 3.95e-38

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: 140.47  E-value: 3.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3222 VGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGC-YMFKIDDNLVVDATMRGNAARFINHCC 3300
Cdd:cd10531    2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGKSNfYILSLSDDVVIDATRKGNLSRFINHSC 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17136558 3301 EPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFE-DEKIPCSCGSKRCR 3354
Cdd:cd10531   82 EPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNYnEAKQVCLCGAQNCR 136
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 1369-1473 2.90e-37

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2B. KMT2B is also called trithorax homolog 2 or WW domain-binding protein 7 (WBP-7). KMT2B is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation by 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. KMT2B contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, this ePHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277164  Cd Length: 105  Bit Score: 136.71  E-value: 2.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGE 1448
Cdd:cd15694    1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                         90       100
                 ....*....|....*....|....*
gi 17136558 1449 HYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15694   81 NFHFMCARASRCCFQDDKKVFCQKH 105
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 3231-3357 1.74e-36

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: 136.01  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3231 GRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRG-IGCYMFKIDDNLVVDATMRGNAARFINHCCEPNCYSKVV 3309
Cdd:cd19175   11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGeKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 17136558 3310 DILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCRKYL 3357
Cdd:cd19175   91 QVDGETRIGVFAIRDIKKGEELTYDYQFVQFGADQDCHCGSKNCRGKL 138
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 3222-3357 2.67e-34

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: 129.62  E-value: 2.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3222 VGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMF-KIDDNLVVDATMRGNAARFINHCC 3300
Cdd:cd19172    4 VEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFmALKSDEIIDATKKGNLSRFINHSC 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3301 EPNCYSK--VVDilGHKHIIIFALRRIVQGEELTYDYKFP-FEDEKIPCSCGSKRCRKYL 3357
Cdd:cd19172   84 EPNCETQkwTVN--GELRVGFFAKRDIPAGEELTFDYQFErYGKEAQKCYCGSPNCRGYI 141
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 3222-3335 3.66e-34

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: 128.52  E-value: 3.66e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3222 VGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGcYMFKIDDNLVVDATMRGNAARFINHCCE 3301
Cdd:cd10519    3 LLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSN 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 17136558 3302 PNCYSKVVDILGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd10519   82 PNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDY 115
PHD3_KMT2A_like cd15508
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 1055-1111 5.31e-34

PHD finger 3 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 third PHD finger.


Pssm-ID: 276983  Cd Length: 57  Bit Score: 125.64  E-value: 5.31e-34
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCPICQRCYDDNDFDLKMMECGDCGQWVHSKCEGLSDEQYNLLSTLPESIEFICKKC 1111
Cdd:cd15508    1 YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC 57
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 3224-3358 6.56e-34

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: 128.56  E-value: 6.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKR--ERYYDSRGIgcYMFKIDDNLVVDATMRGNAARFINHCCE 3301
Cdd:cd19174    4 RFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRmiEQYHNHSHH--YCLNLDSGMVIDGYRMGNEARFVNHSCD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136558 3302 PNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKF-PF-EDEKIPCSCGSKRCRKYLN 3358
Cdd:cd19174   82 PNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFhSFnVEKQQPCKCGSPNCRGVIG 140
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 3231-3336 9.30e-32

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: 121.48  E-value: 9.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   3231 GRGLYCTKDIEAGEMVIEYAGE-LIRSTLTDKRERYY----DSRGIGCYMFKIDDN--LVVDAT--MRGNAARFINHCCE 3301
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYydklELRLWGPYLFTLDEDseYCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 17136558   3302 PNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYK 3336
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 3224-3357 1.12e-31

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: 122.42  E-value: 1.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKR-ERYYDSRGIGCYMFKIDDNLVVDATMRGNAARFINHCCEP 3302
Cdd:cd19173    6 PFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRlKKAHENNITNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 3303 NCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFE-DEKIPCSCGSKRCRKYL 3357
Cdd:cd19173   86 NCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNLDCLgNEKKVCRCGAPNCSGFL 141
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 1369-1473 1.84e-29

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.


Pssm-ID: 277167  Cd Length: 105  Bit Score: 114.76  E-value: 1.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGE 1448
Cdd:cd15697    1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                         90       100
                 ....*....|....*....|....*
gi 17136558 1449 HYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15697   81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 3224-3357 2.36e-29

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: 119.32  E-value: 2.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHiHGRG--LYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIgCYMFKIDDN-----LVVDATMRGNAARFI 3296
Cdd:cd10542   91 IFRTS-NGRGwgVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDYNdddceYTVDAAYYGNISHFI 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136558 3297 NHCCEPN-----CYSKVVDILGHkHIIIFALRRIVQGEELTYDYKF------------PFEDEKIPCSCGSKRCRKYL 3357
Cdd:cd10542  169 NHSCDPNlavyaVWINHLDPRLP-RIAFFAKRDIKAGEELTFDYLMtgtggssestipKPKDVRVPCLCGSKNCRKYL 245
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 1369-1473 1.82e-28

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.


Pssm-ID: 277168  Cd Length: 107  Bit Score: 111.68  E-value: 1.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGE 1448
Cdd:cd15698    1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                         90       100
                 ....*....|....*....|....*
gi 17136558 1449 HYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15698   81 VYHFACAIRAKCMFFKDKTMLCPMH 105
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 3224-3335 5.78e-28

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: 114.39  E-value: 5.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGiGCYMFKIDD---------NLVVDATMRGNAAR 3294
Cdd:cd10538   93 VFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSG-GSYLFDLDEfsdsdgdgeELCVDATFCGNVSR 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17136558 3295 FINHCCEPNC--YSKVVDILGHK--HIIIFALRRIVQGEELTYDY 3335
Cdd:cd10538  172 FINHSCDPNLfpFNVVIDHDDLRypRIALFATRDILPGEELTFDY 216
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 3020-3108 6.95e-28

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region (FYRN), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.


Pssm-ID: 197781  Cd Length: 86  Bit Score: 109.31  E-value: 6.95e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558    3020 HLLYEIQSEDGFTYKSSSITEIWEKVFEAVQVARRAHGLtplPEGPLADMGGIQMIGLKTNALKYLIEQLPGVEKCSKYT 3099
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADL---LQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYW 77


                    ....*....
gi 17136558    3100 PKYHKRNGN 3108
Cdd:smart00542   78 FRYHRSPLL 86
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 3231-3335 1.33e-26

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: 107.66  E-value: 1.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3231 GRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRER-YYDSRGIGCYMFKIDDN---LVVDATMR-GNAARFINH-CCEPNC 3304
Cdd:cd10528   28 GRGVIATRPFEKGDFVVEYHGDLITITEAKKREAlYAKDPSTGCYMYYFQYKgktYCVDATKEsGRLGRLINHsKKKPNL 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17136558 3305 YSKVVDILGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd10528  108 KTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 3222-3357 1.79e-26

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation.


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 107.32  E-value: 1.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3222 VGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGI-GCYMFKIDDNLVVDATMRGNAARFINHCC 3300
Cdd:cd19210    4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItNFYMLTLDKDRIIDAGPKGNYARFMNHCC 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136558 3301 EPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFP-FEDEKIPCSCGSKRCRKYL 3357
Cdd:cd19210   84 QPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLEcLGNGKTVCKCGAPNCSGFL 141
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 1369-1473 1.08e-25

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has 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.


Pssm-ID: 277046 [Multi-domain]  Cd Length: 112  Bit Score: 104.20  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGeGLSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGSLQ--NVHSAVARGRMIKCTVCGNR-GATVGCNVRS 1445
Cdd:cd15571    1 CALCPRSG-GALKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLEveGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 17136558 1446 CGEHYHYPCARSIDCAFL-----TDKSMYCPAH 1473
Cdd:cd15571   80 CPRSFHVSCAIRAGCLFEfedgpGNFVVYCPKH 112
PHD3_KMT2A cd15592
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1055-1111 2.99e-25

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It 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, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, 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 third PHD finger.


Pssm-ID: 277067  Cd Length: 57  Bit Score: 100.83  E-value: 2.99e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCPICQRCYDDNDFDLKMMECGDCGQWVHSKCEGLSDEQYNLLSTLPESIEFICKKC 1111
Cdd:cd15592    1 FCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCINC 57
PHD3_KMT2B cd15593
PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
 1055-1111 1.27e-24

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B 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. KMT2B contains 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 third PHD finger.


Pssm-ID: 277068  Cd Length: 57  Bit Score: 99.15  E-value: 1.27e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCPICQRCYDDNDFDLKMMECGDCGQWVHSKCEGLSDEQYNLLSTLPESIEFICKKC 1111
Cdd:cd15593    1 YCPICLKCYEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSLPDSVVYSCAPC 57
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 3224-3335 3.92e-24

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: 100.11  E-value: 3.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIH-----GRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDsrgIGCYMFKID-DNLVVDATMRGNAARFIN 3297
Cdd:cd10522    2 VDISMIPnlshnGLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHY---DPLYPFDLNgDILVIDAGKKGNLTRFIN 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17136558 3298 HCCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd10522   79 HSDQPNLELIVRTLKGEQHIGFVAIRDIKPGEELFISY 116
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 3227-3337 1.05e-23

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


Pssm-ID: 380995  Cd Length: 120  Bit Score: 98.83  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3227 SHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDsRGIGCYMFKIDDNLVVDATMRGNAARFINHCCEPNCYS 3306
Cdd:cd19218   11 SDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 89

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17136558 3307 KVVDILGHKHIIIFALRRIVQGEELTYDYKF 3337
Cdd:cd19218   90 KVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 3224-3357 1.28e-23

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: 99.29  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIG-CYMFKIDDNLVVDATMRGNAARFINHCCEP 3302
Cdd:cd19211    6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDIThFYMLTIDKDRIIDAGPKGNYSRFMNHSCQP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 3303 NCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFP-FEDEKIPCSCGSKRCRKYL 3357
Cdd:cd19211   86 NCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDcLGNEKTVCRCGAPNCSGFL 141
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 3018-3103 1.73e-23

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.


Pssm-ID: 461788  Cd Length: 83  Bit Score: 96.52  E-value: 1.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   3018 GPHLLYEIQSEDGFTYKSSSITEIWEKVFEAVQVARRAHGLTPlpeGPLADMGGIQMIGLKTNALKYLIEQLPGVEKCSK 3097
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKL---KLPESISGEDMFGLTHPAVVRLIESLPGAEKCTN 77


                   ....*.
gi 17136558   3098 YTPKYH 3103
Cdd:pfam05965   78 YKFRYG 83
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 3227-3341 3.54e-23

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: 97.83  E-value: 3.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3227 SHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDsRGIGCYMFKIDDNLVVDATMRGNAARFINHCCEPNCYS 3306
Cdd:cd19217   13 SDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 91

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 17136558 3307 KVVDILGHKHIIIFALRRIVQGEELTYDYKFPFED 3341
Cdd:cd19217   92 KVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQAD 126
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 3224-3357 3.38e-22

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: 98.91  E-value: 3.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIrsTLTDKRERYYD-SRGIGCYMFKIDDNL--------VVDATMRGNAAR 3294
Cdd:cd10544   94 VFKTPKKGWGLRTLEFIPKGRFVCEYAGEVI--GFEEARRRTKSqTKGDMNYIIVLREHLssgkvletFVDPTYIGNIGR 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3295 FINHCCEPNCYSKVVDIlgHK---HIIIFALRRIVQGEELTYDYKFPFEDEKI--------------PCSCGSKRCRKYL 3357
Cdd:cd10544  172 FLNHSCEPNLFMVPVRV--DSmvpKLALFAARDIVAGEELSFDYSGEFSNSVEsvtlarqdesksrkPCLCGAENCRGFL 249
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 1369-1473 6.41e-21

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 (TCF-20) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1 and TCF-20. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. TCF-20 is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). Both RAI1 and TCF-20 are strongly enriched in chromatin in interphase HeLa cells, and display low nuclear mobility, and have been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome.


Pssm-ID: 277138  Cd Length: 103  Bit Score: 90.06  E-value: 6.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKsgeglsGEEARLL--YCG--HDCWVHTNCAMWSAEVFEeIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVR 1444
Cdd:cd15668    1 CVFCKR------GPHYKGLgdLFGpyYEVWVHEDCAVWAPGVYL-VGGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHK 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 17136558 1445 SCGEHYHYPCARSIDCAFLTDK-SMYCPAH 1473
Cdd:cd15668   74 GCKAKYHYPCAVESGCQLDEENfSLLCPKH 103
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 3224-3357 1.17e-19

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: 88.06  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKR-ERYYDSRGIGCYMFKIDDNLVVDATMRGNAARFINHCCEP 3302
Cdd:cd19212    6 IIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRiKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 3303 NCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFP-FEDEKIPCSCGSKRCRKYL 3357
Cdd:cd19212   86 NCETQKWTVNGDVRVGLFALCDIPAGMELTFNYNLDcLGNGRTECHCGADNCSGFL 141
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 3224-3354 2.08e-19

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: 90.09  E-value: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERyyDSrgigcYMFKID----DNLVVDATMRGNAARFINHC 3299
Cdd:cd10543   95 LFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRED--DS-----YLFDLDnkdgETYCIDARRYGNISRFINHL 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136558 3300 CEPNCYSKVVDIlGHK-----HIIIFALRRIVQGEELTYDYKFPFEDEK---IPCSCGSKRCR 3354
Cdd:cd10543  168 CEPNLIPVRVFV-EHQdlrfpRIAFFASRDIKAGEELGFDYGEKFWRIKgkyFTCRCGSPKCK 229
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 3224-3357 3.17e-19

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: 90.32  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIgCYMFKID-------DNLVVDATMRGNAARFI 3296
Cdd:cd20073   97 IFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDNVGV-TYLFDLDlfedqvdEYYTVDAQYCGDVTRFI 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3297 NHCCEPN--CYSKVVDILGHK--HIIIFALRRIVQGEELTYDYK-FPFEDE-----------------KIPCSCGSKRCR 3354
Cdd:cd20073  176 NHSCDPNlaIYSVLRDKSDSKiyDLAFFAIKDIPALEELTFDYSgRNNFDQlgfignrsnskyinlknKRPCYCGSANCR 255


                 ...
gi 17136558 3355 KYL 3357
Cdd:cd20073  256 GWL 258
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 3232-3339 6.02e-19

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: 85.40  E-value: 6.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3232 RGLYCTKDIEAGEMVIEYAGELirSTLTDKRERYYDSRGIGCYMF---KIDDN-LVVDATMRGNAARFINHCCEPNCY-S 3306
Cdd:cd10529   17 KGLVATEDISPGEPILEYKGEV--SLRSEFKEDNGFFKRPSPFVFfydGFEGLpLCVDARKYGNEARFIRRSCRPNAElR 94

                         90       100       110
                 ....*....|....*....|....*....|...
gi 17136558 3307 KVVDILGHKHIIIFALRRIVQGEELTYDYKFPF 3339
Cdd:cd10529   95 HVVVSNGELRLFIFALKDIRKGTEITIPFDYDY 127
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1386-1473 7.64e-19

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMTC2C and KMTC2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five plant PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.


Pssm-ID: 277135  Cd Length: 90  Bit Score: 83.52  E-value: 7.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1386 LLYCGhDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGEHYHYPCARSIDCaFLTD 1465
Cdd:cd15665    3 LCNLG-EVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGC-FQDI 80

                         90
                 ....*....|
gi 17136558 1466 KSM--YCPAH 1473
Cdd:cd15665   81 KTLtlFCPEH 90
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 3224-3357 8.49e-19

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: 88.41  E-value: 8.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFR-SHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIgCYMFKID---DNLVVDATMRGNAARFINHC 3299
Cdd:cd10532   88 IFRtSNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGI-TYLFDLDyesDEFTVDAARYGNVSHFVNHS 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 3300 CEPN--CYSKVVDILGHK--HIIIFALRRIVQGEELTYDYKFPFEDE---------------KIPCSCGSKRCRKYL 3357
Cdd:cd10532  167 CDPNlqVFNVFIDNLDTRlpRIALFSTRTIKAGEELTFDYQMKGSGDlssdsidnspakkrvRTVCKCGAVTCRGYL 243
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 3231-3357 1.49e-18

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: 88.03  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3231 GRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIgCYMFKID---DNLVVDATMRGNAARFINHCCEPN--CY 3305
Cdd:cd10525   98 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA-TYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNlqVY 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136558 3306 SKVVDILGHK--HIIIFALRRIVQGEELTYDYKF------------------------PFEDEKIPCSCGSKRCRKYL 3357
Cdd:cd10525  177 NVFIDNLDERlpRIALFATRTIRAGEELTFDYNMqvdpvdaestkmdsnfglaglpgsPKKRVRIECKCGVRSCRKYL 254
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 3224-3357 1.85e-18

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: 88.53  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIH-GRGLYCTKDIEAGEMVIEYAGELIRSTLTD-KRERYYDSRGIGCYMFKID--------------DNLVVDAT 3287
Cdd:cd19473  109 IFRTSDGrGWGVRSTVDIKRGQFVDCYVGEIITPEEAQrRRDAATIAQRKDVYLFALDkfsdpdsldprlrgDPYEIDGE 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3288 MRGNAARFINHCCEPNC--YSKVVDiLGHKHI---IIFALRRIVQGEELTYDY--------KFPFEDEKI----PCSCGS 3350
Cdd:cd19473  189 FMSGPTRFINHSCDPNLriFARVGD-HADKHIhdlAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEkemtKCLCGS 267


                 ....*..
gi 17136558 3351 KRCRKYL 3357
Cdd:cd19473  268 PKCRGYL 274
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 3210-3354 3.30e-18

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: 86.53  E-value: 3.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3210 KYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERyyDSrgigcYMFKIDDN----LVVD 3285
Cdd:cd10535   81 RNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE--DS-----YLFDLDNKdgevYCID 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 3286 ATMRGNAARFINHCCEPNCYSKVVdILGHK-----HIIIFALRRIVQGEELTYDYKFPFEDEK---IPCSCGSKRCR 3354
Cdd:cd10535  154 ARFYGNVSRFINHHCEPNLVPVRV-FMAHQdlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKgklFSCRCGSPKCR 229
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 3210-3354 8.12e-18

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: 85.45  E-value: 8.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3210 KYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERyyDSrgigcYMFKIDDN----LVVD 3285
Cdd:cd10533   81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED--DS-----YLFDLDNKdgevYCID 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 3286 ATMRGNAARFINHCCEPNCYSKVVDILGHK----HIIIFALRRIVQGEELTYDYKFPFEDEK---IPCSCGSKRCR 3354
Cdd:cd10533  154 ARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKskyFTCQCGSEKCK 229
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
 3226-3335 1.26e-17

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: 81.47  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3226 RSHIH-GRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGiGCYMFKIDDNLVVDATMRGNAARFINHCCEP-- 3302
Cdd:cd19168    7 KSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVS-YLYLFEEQEGIWVDAAIYGNLSRYINHATDKvk 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 17136558 3303 --NCYSKVVDILGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd19168   86 tgNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 3226-3335 1.37e-17

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: 79.60  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3226 RSHIHGRGLYCTKDIEAGEMVIEyagelirstltdkreryydsrgigcymfkiddnlvvdatmrgnaARFINHCCEPNCY 3305
Cdd:cd08161    6 TIPGAGFGLFATRDIPKGEVIGL--------------------------------------------ARFINHSCEPNCE 41

                         90       100       110
                 ....*....|....*....|....*....|
gi 17136558 3306 SKVVDILGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd08161   42 FEEVYVGGKPRVFIVALRDIKAGEELTVDY 71
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 3224-3357 9.61e-17

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: 82.21  E-value: 9.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKrERYYDSRGIGCYMFKIDDNL-VVDATMRGNAARFINHCCEP 3302
Cdd:cd10541   96 LFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADK-EGLEMGDEYFANLDHIEESCyIIDAKLEGNLGRYLNHSCSP 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136558 3303 NCYSKVVDILGHKH----IIIFALRRIVQGEELTYDYKF---PFEDEKIPCSCGSKRCRKYL 3357
Cdd:cd10541  175 NLFVQNVFVDTHDLrfpwVAFFASKRIKAGTELTWDYNYevgSVEGKELLCCCGSNECRGRL 236
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 3224-3357 1.67e-16

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: 82.72  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRER-----Y----------------YDSRG-IGCYmfkiddn 3281
Cdd:cd10517  133 VFKTEKKGWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLqygdeYfaeldyievveklkegYESDVeEHCY------- 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3282 lVVDATMRGNAARFINHCCEPNCYSKVVDILGHK----HIIIFALRRIVQGEELTYDYKFPF---EDEKIPCSCGSKRCR 3354
Cdd:cd10517  206 -IIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDlrfpWVAFFASRYIRAGTELTWDYNYEVgsvPGKVLYCYCGSSNCR 284


                 ...
gi 17136558 3355 KYL 3357
Cdd:cd10517  285 GRL 287
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
 1369-1473 2.67e-15

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the two ePHD fingers of PFH6 and the single ePHD finger of PFH11. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. PHF6 contains two non-canonical ePHD fingers. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277143  Cd Length: 116  Bit Score: 74.35  E-value: 2.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEglSGEEARLLYCGHDCWVHTNCAMWSAEVFEEIDGS--------LQNVHSAVARGRMIKCTVCGNRGATVG 1440
Cdd:cd15673    1 CGFCKSGEE--NKETGGKLASGEKIAAHHNCMLFSSGLVQYVSPNendfggfdIEDVKKEIKRGRKLKCNLCKKTGATIG 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17136558 1441 CNVRSCGEHYHYPCARSIDCAFLTDKS-----MYCPAH 1473
Cdd:cd15673   79 CDVKQCKKTYHYHCAKKDDAKIIERNSqgiyrVYCKNH 116
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 1369-1473 2.32e-14

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific PHD finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a PHD finger and a non-canonical ePHD finger, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger.


Pssm-ID: 277139 [Multi-domain]  Cd Length: 112  Bit Score: 71.51  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSG--EGLSGEearlLYCGHDCWVHTNCAMWSAEVF------EEIDGSL-QNVHSAVARGRMIKCTVCGNRGATV 1439
Cdd:cd15669    1 CVLCGRSDddPDKYGE----KLQKDGICAHYFCLLFSSGLPqrgednEGIYGFLpEDIRKEVRRASRLRCFYCKKKGASI 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 17136558 1440 GCNVRSCGEHYHYPCARSIDCA--FLTDKSMYCPAH 1473
Cdd:cd15669   77 GCAVKGCRRSFHFPCGLENGCVtqFFGEYRSFCWEH 112
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 1388-1473 5.38e-14

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.


Pssm-ID: 277166  Cd Length: 90  Bit Score: 69.97  E-value: 5.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1388 YCGhDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGEHYHYPCARSIDcAF--LTD 1465
Cdd:cd15696    5 YCG-ECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAG-TFqdFSR 82


                 ....*...
gi 17136558 1466 KSMYCPAH 1473
Cdd:cd15696   83 RLLLCPTH 90
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
 1391-1473 8.42e-14

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of TCF-20. TCF-20, also termed nuclear factor SPBP, or protein AR1, or stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPRE-binding protein), is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome. As a chromatin-binding protein, TCF-20 plays a role in the regulation of gene expression. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). TCF-20 contains an N-terminal transactivation domain, a novel DNA-binding domain with an AT-hook motif, three nuclear localization signals (NLSs) and a C-terminal ePHD/ADD domain.


Pssm-ID: 277169  Cd Length: 103  Bit Score: 69.94  E-value: 8.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1391 HDCWVHTNCAMWSAEVFEeIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGEHYHYPCARSIDCAFLTDK-SMY 1469
Cdd:cd15699   21 YEFWVHEGCILWANGIYL-VCGRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLNEENfSVR 99


                 ....
gi 17136558 1470 CPAH 1473
Cdd:cd15699  100 CPKH 103
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 1396-1473 1.86e-13

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 68.12  E-value: 1.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   1396 HTNCAMWSAEV-FEEIDG---SLQNVHSAVARGRMIKCTVCGNR-GATVGCNVRSCGEHYHYPCARSIDCAFLTDKS--- 1467
Cdd:pfam13771    1 HVVCALWSPELvQRGNDSmgfPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDEDngt 80


                   ....*...
gi 17136558   1468 --MYCPAH 1473
Cdd:pfam13771   81 fkSYCKKH 88
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 1394-1473 1.86e-13

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome, Potocki-Lupski syndrome, and non-syndromic autism. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP and an ePHD/ADD domain with ability to bind nucleosomes.


Pssm-ID: 277170  Cd Length: 104  Bit Score: 68.75  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1394 WVHTNCAMWSAEVFEeIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGEHYHYPCARSIDCAFLTDK-SMYCPA 1472
Cdd:cd15700   25 WVHEACAVWTTGVYL-VAGKLFGLQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEENfSLRCPK 103


                 .
gi 17136558 1473 H 1473
Cdd:cd15700  104 H 104
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 1369-1473 2.03e-13

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277182 [Multi-domain]  Cd Length: 115  Bit Score: 69.16  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKsgeglsGEEARLLYCG--HDCWVHTNCAMWSAEVFE---------EIDGSLQNVHSAVARGRMIKCTVCGNRGA 1437
Cdd:cd15712    1 CAFCPK------GEEYSIMYFAqeQNIAAHQNCLLYSSGFVEseeynplnlDRRFDVESVLNEIKRGKRLKCNFCRKKGA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 17136558 1438 TVGCNVRSCGEHYHYPCARSIDCAFLTDK-----SMYCPAH 1473
Cdd:cd15712   75 TVGCEERACRRSYHYFCALCDDAAIETDEvrgiyRVFCQKH 115
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 1386-1473 5.80e-13

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 at Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.


Pssm-ID: 277165  Cd Length: 90  Bit Score: 66.86  E-value: 5.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1386 LLYCGhDCWVHTNCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGEHYHYPCArSIDCAFLTD 1465
Cdd:cd15695    3 LCNCG-ECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCA-AASGSFQSM 80

                         90
                 ....*....|
gi 17136558 1466 KS--MYCPAH 1473
Cdd:cd15695   81 KTllLLCPEH 90
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 3224-3357 9.61e-13

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: 71.40  E-value: 9.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLT---------DKRERYYDSRGIGCYMF----KIDDNL-VVDATMR 3289
Cdd:cd10523  112 VFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSRARSpteplppklELPSENEVEVVTSWLILskkrKLRENVcFLDASKE 191

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136558 3290 GNAARFINHCCEPNCYSKVVDILGHKH----IIIFALRRIVQGEELTYDYKF---PFEDEKIPCSCGSKRCRKYL 3357
Cdd:cd10523  192 GNVGRFLNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYSYdagTSPEQEIPCLCGVNKCQKKI 266
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 3224-3335 2.21e-12

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: 69.35  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKR----------ERYYDSRGIG---------------CYMFKI 3278
Cdd:cd10545   90 VFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRsgnddylfdiDNRQTNRGWDggqrldvgmsdgersSAEDEE 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136558 3279 DDNLVVDATMRGNAARFINHCCEPNCYSKVVDILGHK----HIIIFALRRIVQGEELTYDY 3335
Cdd:cd10545  170 SSEFTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDlrlpRVMLFAADNIPPLQELTYDY 230
PHD1_KMT2A_like cd15506
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 900-976 2.26e-12

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: 63.92  E-value: 2.26e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558  900 LCFLCGSTGLDPLIFCACCCEPYHQYCVQDEynlkhgsfedttlmgsllETTVNASTGpssslnqltqrlNWLCPRC 976
Cdd:cd15506    1 LCFLCGSAGLNELLYCSVCCEPYHTFCLEEA------------------ERPLNINKD------------NWCCRRC 47
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 3233-3339 7.09e-12

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: 66.66  E-value: 7.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3233 GLYCTKDIEAGEMVIEYAGELIRST--LTDKRERYYDSRGIGCYMFKIDDN-LVVDATMRGNAARFINHCCEPNC--YSK 3307
Cdd:cd19183   15 GLFADRPIPAGDPIQELLGEIGLQSeyIADPENQYQILGAPKPHVFFHPQSpLYIDTRRSGSVARFIRRSCRPNAelVTV 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 17136558 3308 VVDILGHKHIIIFALRRIVQGEELTYDYKFPF 3339
Cdd:cd19183   95 ASDSGSVLKFVLYASRDISPGEEITIGWDWDN 126
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 3230-3335 5.59e-11

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: 62.40  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3230 HGRGLYCTKDIEAGEMVIEYAgELIrSTLTDKRERYYDSRGIGCYMFKIddnlvvdatmrgnaARFINHCCEPNCyskVV 3309
Cdd:cd20071    9 KGRGLVATRDIEPGELILVEK-PLV-SVPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA---VV 69

                         90       100
                 ....*....|....*....|....*.
gi 17136558 3310 DILGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd20071   70 VFDGNGTLRVRALRDIKAGEELTISY 95
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 1369-1455 1.11e-10

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the first ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. .


Pssm-ID: 277180  Cd Length: 115  Bit Score: 61.52  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGE----EARLLYCGHDCWVHTNCAMWSAEVFEEIDG-SLQNVHSAVARGRMIKCTVCGNRGATVGCNV 1443
Cdd:cd15710    1 CGFCRSNREKECGQllisENQKVAAHHKCMLFSSALVSSHSDSENLGGfSIEDVQKEIKRGTKLMCSLCHCPGATIGCDV 80

                         90
                 ....*....|..
gi 17136558 1444 RSCGEHYHYPCA 1455
Cdd:cd15710   81 KTCHRTYHYYCA 92
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1055-1114 6.16e-10

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: 57.12  E-value: 6.16e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   1055 FCPICQRCYDDNDfdlkMMECGDCGQWVHSKCEGLSDEQYNLLSTlpesiEFICKKCARR 1114
Cdd:pfam00628    1 YCAVCGKSDDGGE----LVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPECKPK 51
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 1522-1569 1.48e-09

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.


Pssm-ID: 461787  Cd Length: 51  Bit Score: 55.97  E-value: 1.48e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 17136558   1522 GSLEVRQLGAIVPRFSDSY--EAVVPINFLCSRLYWSSKEPWKIVEYTVR 1569
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPAFHteRYIYPVGYKSTRLYWSTKDPRKRCRYTCE 50
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
 1529-1574 1.24e-08

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region (FYRC), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.


Pssm-ID: 128814  Cd Length: 44  Bit Score: 53.06  E-value: 1.24e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 17136558    1529 LGAIVPRFSDSYEAVVPINFLCSRLYWSSKEPWKIVEYtvRTTIQN 1574
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLY--SCVIDE 44
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
 1055-1111 1.75e-08

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 (ARID4) and similar proteins; This family includes A. thaliana ARID4 (ARID domain-containing protein 4) and similar proteins. Their biological roles remain unclear, but they all contain an AT-rich interactive domain (ARID) and a plant homeodomain (PHD) finger at the C-terminus. ARID is a helix-turn-helix motif-based DNA-binding domain conserved in all eukaryotes. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277087  Cd Length: 57  Bit Score: 53.25  E-value: 1.75e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136558 1055 FCPICQRCYDDNDFDLK-MMECGDCGQWVHSKCE---GLSDEQYnllsTLPESIEFICKKC 1111
Cdd:cd15615    1 FCILCGQVYEENEGDEKeWVQCDSCSEWVHFECDgrtGLGAFKY----AKSDGLQYVCPRC 57
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1055-1111 3.66e-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: 51.83  E-value: 3.66e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558    1055 FCPICQRCYDDNDfdlkMMECGDCGQWVHSKCEGLSDEQYNLLStlpesiEFICKKC 1111
Cdd:smart00249    1 YCSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLLEEEPDG------KWYCPKC 47
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 1411-1473 5.05e-08

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the second ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4.


Pssm-ID: 277181  Cd Length: 118  Bit Score: 53.93  E-value: 5.05e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136558 1411 DGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVRSCGEHYHYPCARSIDCAFLTDKS-----MYCPAH 1473
Cdd:cd15711   51 DFDIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGVQDKAKYIENMSrgiykLYCKNH 118
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 1055-1111 1.23e-07

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: 50.39  E-value: 1.23e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCPICQRCYDDNDfdlKMMECGDCGQWVHSKCEGLSdeqynlLSTLPESIEFICKKC 1111
Cdd:cd15489    1 SCIVCGKGGDLGG---ELLQCDGCGKWFHADCLGPP------LSSFVPNGKWICPVC 48
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 3224-3353 1.60e-07

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: 53.47  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYdSRGIGCYMFKIDDN---LVVDATMRGNAARFINHCC 3300
Cdd:cd19181   11 VTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGHFF-KRPYPFVLFYSKFNgveMCVDARTFGNDARFIRRSC 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 3301 EPNCYSKVVDILGHKHIIIFALRRIVQGEELT--YDYKFPFEDEKIPCSC--GSKRC 3353
Cdd:cd19181   90 TPNAEVRHMIADGMIHLCIYAVAAIAKDAEVTiaFDYEYSNCNYKVDCAChkGNRNC 146
PHD1_KMT2A cd15588
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 900-929 1.28e-06

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It 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 MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, 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: 277063  Cd Length: 47  Bit Score: 47.64  E-value: 1.28e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 17136558  900 LCFLCGSTGLDPLIFCACCCEPYHQYCVQD 929
Cdd:cd15588    1 VCFLCASSGHVEFVYCQVCCEPFHKFCLEE 30
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 3224-3335 1.41e-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: 49.56  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3224 VFRSHIHGRGLYCTKDIEAGEmVIEYAGELIRStltdkRERYYDSRG--IGCYMFKIDDNLVvdATMRGNAARFiNHCCE 3301
Cdd:cd10540    4 VKPSTLKGRGVFATRPIKKGE-VIEEAPVIVLP-----KEEYQHLCKtvLDHYVFSWGDGCL--ALALGYGSMF-NHSYT 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 17136558 3302 PNCYsKVVDIlGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd10540   75 PNAE-YEIDF-ENQTIVFYALRDIEAGEELTINY 106
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
 1394-1473 2.17e-06

Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the ePHD finger of the family of BRPF proteins, which includes BRPF1, BRD1/BRPF2, and BRPF3. These are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.


Pssm-ID: 277140  Cd Length: 116  Bit Score: 49.26  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1394 WVHTNCAMWSAEV-------FEEIDGsLQNVhsAVARGRMiKCTVCGNR-GATVGCNVRSCGEHYHYPCAR--------- 1456
Cdd:cd15670   19 WAHVVCALWIPEVsfantvfLEPIDG-IQNI--PKARWKL-TCYICKKRmGACIQCHKKNCYTAFHVTCAQqaglymkie 94

                         90       100
                 ....*....|....*....|..
gi 17136558 1457 -----SIDCAFLTDKSMYCPAH 1473
Cdd:cd15670   95 pvkdpGNGTSDSVRKEAYCDKH 116
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
 1055-1111 2.54e-06

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: 46.51  E-value: 2.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCPICQRCYDDNDfdlkMMECGDCGQWVHSKCEGLSDEQynllstlPESIEFICKKC 1111
Cdd:cd15522    1 ICPICKKPDDGSP----MIGCDECDDWYHWECVGITDEP-------PEEDDWFCPKC 46
PHD1_KMT2B cd15589
PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
 900-929 6.90e-06

PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B 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. KMT2B contains 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: 277064  Cd Length: 47  Bit Score: 45.62  E-value: 6.90e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 17136558  900 LCFLCGSTGLDPLIFCACCCEPYHQYCVQD 929
Cdd:cd15589    1 VCLLCASKGQHELLFCQVCCEPFHRFCLEE 30
ePHD_ATX1_2_like cd15662
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...
 1394-1457 7.12e-06

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 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 known as 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 known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain.


Pssm-ID: 277132  Cd Length: 115  Bit Score: 47.47  E-value: 7.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136558 1394 WVHTNCAMWSAE--VFEEIDGSLQNVHSAVARGRM-IKCTVCGNR-GATVGCNVRSCGEHYHYPCARS 1457
Cdd:cd15662   19 WAHLACAIWIPEtcLLDVKTMEPVDGINAISKERWeLSCTICKQRyGACIQCSNNSCRVAYHPLCARA 86
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 1056-1111 8.57e-06

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. 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 interaction 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. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 45.23  E-value: 8.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 1056 CPICQRCYDDNDFDlkMMECGDCGQWVHSKCEGLSDEQYNLLStlpesiEFICKKC 1111
Cdd:cd15517    2 CGICNLETAAVDEL--WVQCDGCDKWFHQFCLGLSNERYADED------KFKCPNC 49
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 3230-3355 9.45e-06

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


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 48.05  E-value: 9.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3230 HGRGLYCTKDIEAGEmVIEYAGELIrSTLTDKRERYYDSRGigcymfkiDDNLVVDATMRGNA------ARFINHCCEPN 3303
Cdd:cd10524   18 YGAKIIATKPIKKGE-KIHELCGCI-AELSEEEEALLRPGG--------NDFSVMYSSRKKCSqlwlgpAAFINHDCRPN 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17136558 3304 CysKVVDIlGHKHIIIFALRRIVQGEELTYDY--KFpFEDEKIPCSCGSkrCRK 3355
Cdd:cd10524   88 C--KFVPT-GKSTACVKVLRDIEPGEEITVYYgdNY-FGENNEECECET--CER 135
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
 1058-1111 1.43e-05

PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, Dido2, and Dido3; PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. This family also includes Dido gene encoding three alternative splicing variants (Dido1, 2, and 3), which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1 is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved PHD finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine4 (H3K4me3). Gene Dido1 is a Bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform and is ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but is involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, a SPOC module, and a long C-terminal region (CT) of unknown homology.


Pssm-ID: 277027  Cd Length: 50  Bit Score: 44.70  E-value: 1.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17136558 1058 ICQRCYDdNDFdlkMMECGDCGQWVHSKCEGLSDEQYNLLSTlpESIEFICKKC 1111
Cdd:cd15552    3 ICRKPHN-NRF---MICCDRCEEWFHGDCVGITEAQGKEMEE--NIEEYVCPKC 50
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 978-1022 1.66e-05

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: 44.51  E-value: 1.66e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 17136558     978 VCYTCNMS--SGSKVKCQKCQKNYHSTCLGTSKRLLGADRPLICVNC 1022
Cdd:smart00249    1 YCSVCGKPddGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PRK13914 PRK13914
invasion associated endopeptidase;
638-856 2.39e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 49.80  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   638 TQAGTKKSGAAEAQVEEVQPQKEEAPQTSTTTQPSASNGASHGVPQAELAGE-----TNAT------GDTLKRQRIDLkG 706
Cdd:PRK13914  140 TDKVTSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAPKVAETKEtpvvdQNATthavksGDTIWALSVKY-G 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   707 PRVKHV-----CRSASIVLGQPLATfgedQQPEDAADMQQEIAAPVPSAimepspEKPTHIVTDENDNCASCKTspvgdE 781
Cdd:PRK13914  219 VSVQDImswnnLSSSSIYVGQKLAI----KQTANTATPKAEVKTEAPAA------EKQAAPVVKENTNTNTATT-----E 283

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136558   782 SKpsKSSGSAQAEVKKATALGKEGTASAAGGSSAKVTTRNAAVASNLIVAASKKQRNGDIATSSSVTQSSNQTQG 856
Cdd:PRK13914  284 KK--ETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQG 356
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
 3234-3339 2.49e-05

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: 46.42  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3234 LYCTKDIEAGEMVIEYAGELIrstLTDKRER--YYDSRGIGCYMF--KIDD-NLVVDATMRGNAARFINHCCEPNCYSKV 3308
Cdd:cd19182   21 LKAAKDLPPDTLIIEYRGKFM---LREQFEAngYFFKRPYPFVLFysKFHGlEMCVDARTFGNEARFIRRSCTPNAEVRH 97

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17136558 3309 VDILGHKHIIIFALRRIVQGEELTYDYKFPF 3339
Cdd:cd19182   98 VIEDGTIHLYIYSIRSIPKGTEITIAFDFDY 128
PHD2_NSD cd15565
PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 1429-1473 2.54e-05

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: 43.96  E-value: 2.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 17136558 1429 CTVCGNRGATVG----CNVRSCGEHYHYPCARSIDCAFLTD-KSMYCPAH 1473
Cdd:cd15565    2 CFVCKKLGSVGGevfkCSVASCGKFYHEECLKKWPLTTISDsKKFRCPLH 51
PHD_PHF2_like cd15554
PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar ...
 1055-1111 3.34e-05

PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar proteins. PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20(H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. All family members contain a plant homeodomain (PHD) finger and a JmjC domain.


Pssm-ID: 277029  Cd Length: 47  Bit Score: 43.53  E-value: 3.34e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1055 FCpICQRCYDDNDFdlkMMECGDCGQWVHSKCEGLSDEQYNLLstlpesIEFICKKC 1111
Cdd:cd15554    1 YC-ICRQPYDVTRF---MIECDVCKDWFHGSCVGVEEHQANDI------ERYHCPNC 47
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
 3237-3335 4.23e-05

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: 45.86  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3237 TKDIEAGEMVIEYAGEL--IRSTLTDKReryyDSrgIGCYMFKID--DNLVVDATMRGNAARFI----NHCCE----PNC 3304
Cdd:cd10539   21 DGFIKDLTIIAEYTGDVdyIRNREFDDN----DS--IMTLLLAGDpsKSLVICPDKRGNIARFIsginNHTKDgkkkQNC 94

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17136558 3305 YSKVVDILGHKHIIIFALRRIVQGEELTYDY 3335
Cdd:cd10539   95 KCVRYSINGEARVLLVATRDIAKGERLYYDY 125
NR_DBD_TLX cd07163
DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers; DNA-binding ...
 394-488 4.47e-05

DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers; DNA-binding domain of Tailless (TLX) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. TLX interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. TLX is an orphan receptor that is expressed by neural stem/progenitor cells in the adult brain of the subventricular zone (SVZ) and the dentate gyrus (DG). It plays a key role in neural development by promoting cell cycle progression and preventing apoptosis in the developing brain. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TLX has a central well conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 143537  Cd Length: 92  Bit Score: 44.79  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558  394 CSICSAVVSSKEvtqarkYGVVACDVCRKFFskmtKKSISANsstantssgsQQYLqCKGNEGSPCSIhsaksqlknfKK 473
Cdd:cd07163    9 CKVCGDRSSGKH------YGIYACDGCSGFF----KRSIRRN----------RQYV-CKSKGQGGCPV----------DK 57

                         90
                 ....*....|....*
gi 17136558  474 FYKDRCTACWLKKCM 488
Cdd:cd07163   58 THRNQCRACRLKKCF 72
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 3221-3335 4.84e-05

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.


Pssm-ID: 380928  Cd Length: 130  Bit Score: 45.75  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 3221 YVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIgcymfKIDDNLVVD------------ATM 3288
Cdd:cd10530   10 YVAESLIPSAGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTI-----SLDEETVIDvpepynsvskycASL 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17136558 3289 rGNAArfiNHCCEPNCyskVVDILGHK---HI-IIFALRRIVQGEELTYDY 3335
Cdd:cd10530   85 -GHKA---NHSFTPNC---IYDPFVHPrfgPIkCIRTLRAVEAGEELTVAY 128
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 1369-1473 5.40e-05

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins 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, has 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 PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277141  Cd Length: 112  Bit Score: 45.13  E-value: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGL----SGEEarllycghdcWVHTNCAMWSAEV-------FEEIDgslqNV-HSAVARGRMIkCTVCGNR- 1435
Cdd:cd15671    1 CVLCPKKGGAMkstkSGTK----------WVHVSCALWIPEVsigcpekMEPIT----KIsHIPMSRWALV-CVLCKEKt 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17136558 1436 GATVGCNVRSCGEHYHypcarsIDCAFLTDKSM---------------YCPAH 1473
Cdd:cd15671   66 GACIQCSVKSCKTAFH------VTCAFQHGLEMktilededdevkfksYCPKH 112
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1429-1473 8.41e-05

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: 42.58  E-value: 8.41e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 17136558    1429 CTVCG---NRGATVGCNvrSCGEHYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:smart00249    2 CSVCGkpdDGGELLQCD--GCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PHD6_KMT2C_like cd15514
PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in ...
 1056-1111 9.87e-05

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in KMT2D; KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the sixth PHD finger of KMT2C and the fifth PHD finger of KMT2D.


Pssm-ID: 276989  Cd Length: 51  Bit Score: 42.27  E-value: 9.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1056 CPICQRCYDDNDfdlKMMECGDCGQWVHSKCEGL-SDEQYNLLStlpeSIEFICKKC 1111
Cdd:cd15514    2 CPVCSRSYNEGE---LIIQCSQCERWLHGACDSLrTEEEAERAA----DNGYRCLLC 51
ePHD_JADE3 cd15706
Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...
 1369-1455 1.02e-04

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-3. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is close 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 PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.


Pssm-ID: 277176  Cd Length: 111  Bit Score: 44.33  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLycghdcWVHTNCAMWSAEVF----EEIDGSLQNVHSAVARGRMIkCTVCGNR-GATVGCNV 1443
Cdd:cd15706    1 CLLCPKTGGAMKATRTGTK------WAHVSCALWIPEVSiacpERMEPITKVSHIPPSRWALV-CSLCKLKtGACIQCSV 73

                         90
                 ....*....|..
gi 17136558 1444 RSCGEHYHYPCA 1455
Cdd:cd15706   74 KSCITAFHVTCA 85
PHD3_KMT2C cd15511
PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
 1056-1111 2.05e-04

PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains. This model corresponds to the third PHD finger.


Pssm-ID: 276986  Cd Length: 52  Bit Score: 41.32  E-value: 2.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 1056 CPICQRCYDDNdFDLKMMECGDCGQWVHSKCEGLSDEQynLLSTLPEsiEFICKKC 1111
Cdd:cd15511    2 CPACKKNLDPE-LQKDMLHCHVCKRWIHLECEKPNDNE--LLDQLKE--DYICSLC 52
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
1391-1473 2.12e-04

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 43.10  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558   1391 HDCWVHTNCAMWSAEVF-------EEIDgsLQNVHSAVARGrmiKCTVCGNR-GATVGCNVRSCGEHYHYPCARS----- 1457
Cdd:pfam13832   18 DGRWVHVLCAIFVPEVRfgnvatmEPID--VSRIPPERWKL---KCVFCKKRsGACIQCSKGRCTTAFHVTCAQAagvym 92

                           90
                   ....*....|....*..
gi 17136558   1458 -IDCAFLTDKSMYCPAH 1473
Cdd:pfam13832   93 ePEDWPNVVVIAYCQKH 109
PHD_PYGO cd15551
PHD finger found in PYGO proteins; The family includes Drosophila melanogaster protein pygopus ...
 1056-1111 2.57e-04

PHD finger found in PYGO proteins; The family includes Drosophila melanogaster protein pygopus (dPYGO) and its two homologs, PYGO1 and PYGO2. dPYGO is a fundamental Wnt signaling transcriptional component in Drosophila. PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts an adaptor between Pygopus (Pygo) and Arm/beta-catenin. dPYGO and PYGO2 function as context-dependent beta-catenin coactivators, and they bind di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). Moreover, PYGO2 acts as a histone methylation reader, and a chromatin remodeler in a testis-specific and Wnt-unrelated manner. It also mediates chromatin regulation and links Wnt signaling and Notch signaling to suppress the luminal/alveolar differentiation competence of mammary stem and basal cells. PYGO2 also plays a new role in rRNA transcription during cancer cell growth. It regulates mammary tumor initiation and heterogeneity in MMTV-Wnt1 mice. All family members contain a plant homeodomain (PHD) finger.


Pssm-ID: 277026  Cd Length: 54  Bit Score: 41.20  E-value: 2.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558 1056 CPICQRCYDDNDfdlKMMEC-GDCGQWVHSKCEGLSDEQYNLLsTLPESIEFICKKC 1111
Cdd:cd15551    2 CGICNNEVNDDD---DAILCeSSCNKWFHRTCTGLTESAYDLL-TSEESAEWVCDSC 54
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 975-1022 2.61e-04

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 41.15  E-value: 2.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 17136558  975 RCTVCYTCNMSSGSKVKCQKCQKNYHSTCLGTSKRLLGADRPLICVNC 1022
Cdd:cd15489    1 SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48
PHD2_KMT2B cd15591
PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
 976-1022 3.21e-04

PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B 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. KMT2B contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD), 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 second PHD finger.


Pssm-ID: 277066  Cd Length: 50  Bit Score: 40.69  E-value: 3.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 17136558  976 CTVCYTCNMSSGSKVKCQKCQKNYHSTCLGTS--KRLLGADRPLICVNC 1022
Cdd:cd15591    2 CHVCGRKNKESKPLLECERCRNCYHPACLGPNypKPANRKKRPWICSAC 50
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 901-976 4.02e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 40.66  E-value: 4.02e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136558     901 CFLCGST-GLDPLIFCACCCEPYHQYCVQDEYNLKhgsfedttlmgsllettvnastgpssslnqlTQRLNWLCPRC 976
Cdd:smart00249    2 CSVCGKPdDGGELLQCDGCDRWYHQTCLGPPLLEE-------------------------------EPDGKWYCPKC 47
PHD_PHF3 cd15638
PHD finger found in PHD finger protein 3 (PHF3); PHF3 is a human homolog of yeast protein ...
 1056-1111 7.31e-04

PHD finger found in PHD finger protein 3 (PHF3); PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain.


Pssm-ID: 277108  Cd Length: 51  Bit Score: 39.91  E-value: 7.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 1056 CPICQRCYDdNDFdlkMMECGDCGQWVHSKCEGLSDEQYNLLSTlpESIEFICKKC 1111
Cdd:cd15638    2 CGFCKKPHG-NRF---MVGCGRCDDWFHGDCVGLSLSQAQQMEE--EDKEYVCVKC 51
NR_DBD_PNR_like cd07154
The DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) nuclear ...
 394-488 9.49e-04

The DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) nuclear receptor-like family; The DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) nuclear receptor-like family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. PNR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. This family includes nuclear receptor Tailless (TLX), photoreceptor cell-specific nuclear receptor (PNR) and related receptors. TLX is an orphan receptor that plays a key role in neural development by regulating cell cycle progression and exit of neural stem cells in the developing brain. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PNR-like receptors have a central well-conserved DNA-binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 143529  Cd Length: 73  Bit Score: 40.25  E-value: 9.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558  394 CSICSAVVSSKEvtqarkYGVVACDVCRKFFskmtKKSISANSStantssgsqqyLQCKGNEGSpCSIHSAKsqlknfkk 473
Cdd:cd07154    1 CKVCGDRSSGKH------YGVYACDGCSGFF----KRSIRRNLL-----------YTCKAGNGS-CVVDKAR-------- 50

                         90
                 ....*....|....*
gi 17136558  474 fyKDRCTACWLKKCM 488
Cdd:cd07154   51 --RNQCQACRLKKCL 63
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
1394-1512 1.24e-03

PHD zinc finger-containing protein [General function prediction only];


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 44.59  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1394 WVHTNCAMWSAEVF-------EEIDGsLQNVHSAVARgrmIKCTVCGNRGAT-VGCNVRSCGEHYHYPCARSiDCAFLT- 1464
Cdd:COG5141  268 WGHVICAMFNPELSfghllskDPIDN-IASVSSSRWK---LGCLICKEFGGTcIQCSYFNCTRAYHVTCARR-AGYFDLn 342

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136558 1465 -----------DKSMYCPAHAK----NGNALKANGSPSVtYESNFEVSRPVYVELDRKRKKLI 1512
Cdd:COG5141  343 iyshngisyciDHEPLCRKHYPlgygRMNGLRYFGYEKL-RYKNPPTAIPRKVRAARPRATLF 404
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
 1369-1474 1.52e-03

Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1. Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the Serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation and ASA transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277174  Cd Length: 118  Bit Score: 41.21  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEARLLycghdcWVHTNCAMWSAEVF----EEIDGSLQNVHSAVARGRMIkCTVCGNR-GATVGCNV 1443
Cdd:cd15704    4 CLLCPKKGGAMKPTRSGTK------WVHVSCALWIPEVSigspEKMEPITKVSHIPSSRWALV-CSLCNEKvGASIQCSV 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 17136558 1444 RSCGEHYHYPCA--RSIDCAFLTDKS------MYCPAHA 1474
Cdd:cd15704   77 KNCRTAFHVTCAfdRGLEMKTILAENdevkfkSYCPKHS 115
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 901-979 1.57e-03

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 39.01  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558    901 CFLCGSTGLD-PLIFCACCCEPYHQYCVQ---DEYNLKHGsfedttlmgsllettvnastgpssslnqltqrlNWLCPRC 976
Cdd:pfam00628    2 CAVCGKSDDGgELVQCDGCDDWFHLACLGpplDPAEIPSG---------------------------------EWLCPEC 48


                   ...
gi 17136558    977 TVC 979
Cdd:pfam00628   49 KPK 51
PHD_UBR7 cd15542
PHD finger found in putative E3 ubiquitin-protein ligase UBR7; UBR7, also termed N-recognin-7, ...
 1055-1111 1.78e-03

PHD finger found in putative E3 ubiquitin-protein ligase UBR7; UBR7, also termed N-recognin-7, is a UBR box-containing protein that belongs to the E3 ubiquitin ligase family that recognizes N-degrons or structurally related molecules for ubiquitin-dependent proteolysis or related processes through the UBR box motif. In addition to the UBR box, UBR7 also harbors a plant homeodomain (PHD) finger. The biochemical properties of UBR7 remain unclear.


Pssm-ID: 277017  Cd Length: 54  Bit Score: 38.89  E-value: 1.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136558 1055 FCpICQRCYDDNDFDLK--MMECGDCGQWVHSKCEGLSDEQYNllstLPESIEFICKKC 1111
Cdd:cd15542    1 YC-TCDRPYPDPEDEVEdeMIQCVLCEDWFHGRHLGLTPPEPD----PDEFDEMICSGC 54
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
 1369-1455 2.07e-03

Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-2. Jade-2, also termed PHD finger protein 15 (PHF15), 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-2 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. Jade-2 contains a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277175  Cd Length: 111  Bit Score: 40.46  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGL----SGEEarllycghdcWVHTNCAMWSAEVF----EEIDGSLQNVHSAVARGrMIKCTVCGN-RGATV 1439
Cdd:cd15705    1 CLLCPKRGGALkptrSGTK----------WVHVSCALWIPEVSigcpEKMEPITKISHIPASRW-ALSCSLCKEcTGTCI 69

                         90
                 ....*....|....*.
gi 17136558 1440 GCNVRSCGEHYHYPCA 1455
Cdd:cd15705   70 QCSMPSCITAFHVTCA 85
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
 1394-1473 2.37e-03

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF3. BRF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.


Pssm-ID: 277173 [Multi-domain]  Cd Length: 118  Bit Score: 40.42  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1394 WVHTNCAMWSAEV-------FEEIDGsLQNVHSAVARgrmIKCTVCGN--RGATVGCNVRSCGEHYHYPCAR------SI 1458
Cdd:cd15703   19 WAHVVCAIWIPEVcfantvfLEPVEG-VNNIPPARWK---LTCYLCKQkgRGAAIQCHKVNCYTAFHVTCAQraglfmKI 94

                         90       100
                 ....*....|....*....|....
gi 17136558 1459 D---------CAFLTDKSMYCPAH 1473
Cdd:cd15703   95 EpvretglngTTFTVRKTAYCENH 118
NR_DBD_PNR_like_1 cd07164
DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like proteins is ...
 394-488 3.32e-03

DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like proteins is composed of two C4-type zinc fingers; DNA-binding domain of the photoreceptor cell-specific nuclear receptor (PNR) like proteins is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. PNR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. PNR is a member of nuclear receptor superfamily of the ligand-activated transcription factors. PNR is expressed only in the outer layer of retinal photoreceptor cells. It may be involved in the signaling pathway regulating photoreceptor differentiation and/or maintenance. It most likely binds to DNA as a homodimer. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PNR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 143538  Cd Length: 78  Bit Score: 38.98  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558  394 CSICSAVVSSKEvtqarkYGVVACDVCRKFFskmtKKSISANSStantssgsqqyLQCKgnEGSPCSIHSAKsqlknfkk 473
Cdd:cd07164    1 CRVCGDRASGKH------YGVPSCDGCRGFF----KRSIRRNLA-----------YVCK--ENGSCVVDVAR-------- 49

                         90
                 ....*....|....*
gi 17136558  474 fyKDRCTACWLKKCM 488
Cdd:cd07164   50 --RNQCQACRFKKCL 62
PHD2_KMT2A_like cd15507
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 976-1022 3.90e-03

PHD finger 2 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 second PHD finger.


Pssm-ID: 276982  Cd Length: 50  Bit Score: 37.83  E-value: 3.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 17136558  976 CTVCYTCNMSSGSKVKCQKCQKNYHSTCLGTS--KRLLGADRPLICVNC 1022
Cdd:cd15507    2 CHVCGRKGQAQKQLLECEKCQRGYHVDCLGPSypTKPTRKKKTWICSKC 50
PHD_KDM2A_2B cd15555
PHD finger found in Lysine-specific demethylase KDM2A, KDM2B, and similar proteins; This ...
 1056-1111 4.54e-03

PHD finger found in Lysine-specific demethylase KDM2A, KDM2B, and similar proteins; This family includes KDM2A, KDM2B, and F-box and leucine-rich repeat protein 19 (FBXL19). KDM2A is a ubiquitously expressed histone H3 lysine 36 (H3K36) demethylase that has been implicated in gene silencing, cell cycle, cell growth, and cancer development. KDM2B is a ubiquitously expressed histone H3 lysine 4 (H3K4me2) or histone H3 lysine 36 (H3K36me2) demethylase that functions as a regulator of chemokine expression, cellular morphology, and the metabolome of fibroblasts. Both KDM2A and KDM2B belong to the JmjC-domain-containing histone demethylase family. They consist of two Jumonji C (JmjC) domains, and FBXHA and FBXHB domains. A CXXC zinc-finger domain, followed by a plant homeodomain (PHD) finger, is located within the FBXHA domain, and an F-box domain, followed by an antagonist of mitotic exit network protein 1 (AMN1) domain, is located within the FBXHB domain. FBXL19 belongs to the Skp1-Cullin-F-box (SCF) family of E3 ubiquitin ligases. It mediates ubiquitination and interleukin 33 (IL-33)-induced degradation of ST2L receptor in lung epithelia, blocks IL-33-mediated apoptosis, and prevents endotoxin-induced acute lung injury. FBXL19 consists of FBXHA and FBXHB domains, similar to KDM2A and KDM2B.


Pssm-ID: 277030  Cd Length: 55  Bit Score: 37.77  E-value: 4.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136558 1056 CPICQRCYDDNDFDLKMMECGDCGQWVHSKCEGLSDEQYNLLSTLPESIEfiCKKC 1111
Cdd:cd15555    2 CLICGEDGKEDEFETTLMECSICWEIVHPECLKEQGEGGVVNEDLPNSWE--CPKC 55
PostSET smart00508
Cysteine-rich motif following a subset of SET domains;
3342-3358 4.69e-03

Cysteine-rich motif following a subset of SET domains;


Pssm-ID: 214703  Cd Length: 17  Bit Score: 36.61  E-value: 4.69e-03
                            10
                    ....*....|....*..
gi 17136558    3342 EKIPCSCGSKRCRKYLN 3358
Cdd:smart00508    1 KKQPCLCGAPNCRGFLG 17
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 1429-1473 6.44e-03

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: 36.92  E-value: 6.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 17136558 1429 CTVCGNRGATVGCNVRSCGEHYHypcarsIDCAFLT---DKSMYCPAH 1473
Cdd:cd15568    2 CFRCGDGGDLVLCDFKGCPKVYH------LSCLGLEkppGGKWICPWH 43
NR_DBD_TR2_like cd06967
DNA-binding domain of the TR2 and TR4 (human testicular receptor 2 and 4) is composed of two ...
 410-488 6.54e-03

DNA-binding domain of the TR2 and TR4 (human testicular receptor 2 and 4) is composed of two C4-type zinc fingers; DNA-binding domain of the TR2 and TR4 (human testicular receptor 2 and 4) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. TR2 and TR4 interact with specific DNA sites upstream of the target gene and modulate the rate of transcriptional initiation. TR4 and TR2 are orphan nuclear receptors; the physiological ligand is as yet unidentified. TR2 is abundantly expressed in the androgen-sensitive prostate. TR4 transcripts are expressed in many tissues, including central nervous system, adrenal gland, spleen, thyroid gland, and prostate. It has been shown that human TR2 binds to a wide spectrum of natural hormone response elements (HREs) with distinct affinities suggesting that TR2 may cross-talk with other gene expression regulation systems. The genes responding to TR2 or TR4 include genes that are regulated by retinoic acid receptor, vitamin D receptor, and peroxisome proliferator-activated receptor. TR4/2 binds to HREs as dimers. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, TR2-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).


Pssm-ID: 143525  Cd Length: 87  Bit Score: 38.21  E-value: 6.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136558  410 RKYGVVACDVCRKFFSKMTKKSISansstantssgsqqyLQCKGNEGspCSIHsaksqlknfkKFYKDRCTACWLKKCM 488
Cdd:cd06967   16 RHYGAVSCEGCKGFFKRSIRKNLG---------------YSCRGSKD--CVIN----------KHHRNRCQYCRLQKCL 67
PHD_ash2p_like cd15583
PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and ...
 1062-1111 6.78e-03

PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and similar proteins; spAsh2p, also termed Set1C component ash2, or COMPASS component ash2, or complex proteins associated with set1 protein ash2, or Lid2 complex component ash2, or Lid2C component ash2, is orthologous to Drosophila melanogaster Ash2 protein. Both spAsh2p and D. melanogaster Ash2 contain a plant homeodomain (PHD) finger and a SPRY domain. In contrast, its counterpart in Saccharomyces cerevisiae, Bre2p, has no PHD finger and is not included in this family. spAsh2p shows histone H3 Lys4 (H3K4) methyltransferase activity through its PHD finger. It also interacts with Lid2p in S. pombe. Human Ash2L contains an atypical PHD finger that lacks part of the Cys4HisCys3 signature characteristic of PHD fingers, it binds to only one zinc ion through the second half of the motif and does not have histone tail binding activity.


Pssm-ID: 277058  Cd Length: 50  Bit Score: 36.94  E-value: 6.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17136558 1062 CYDDNDFDLKMME--CGDCGQWVHSKCEGlsdeqYNLLSTLPESI--EFICKKC 1111
Cdd:cd15583    2 CYCGKDRNLGEVElqCSICLKWFHAKCVS-----IDNGSCLPFMTnyQFVCKRC 50
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 1429-1473 8.43e-03

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 36.91  E-value: 8.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 17136558 1429 CTVCGN----RGATVGCNvrSCGEHYHYPCARSIDCAFLTDKSMYCPAH 1473
Cdd:cd15489    2 CIVCGKggdlGGELLQCD--GCGKWFHADCLGPPLSSFVPNGKWICPVC 48
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
 1369-1473 8.97e-03

Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF2. BRPF2 also termed bromodomain-containing protein 1 (BRD1), or BR140-likeprotein, 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 plant homeodomain (PHD) finger followed by a non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.


Pssm-ID: 277172  Cd Length: 118  Bit Score: 38.87  E-value: 8.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136558 1369 CLFCRKSGEGLSGEEarllycgHDCWVHTNCAMWSAEV-------FEEIDGsLQNVHSAVARgrmIKCTVCGNR--GATV 1439
Cdd:cd15702    1 CVLCPNKGGAFKKTD-------DDRWGHVVCALWIPEVgfantvfIEPIDG-VRNIPPARWK---LTCYLCKQKgvGACI 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 17136558 1440 GCNVRSCGEHYHYPCARSI---------------DCAFLTDKSMYCPAH 1473
Cdd:cd15702   70 QCHKANCYTAFHVTCAQKAglymkmepvkevtggGTTFSVRKTAYCDAH 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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