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Conserved domains on  [gi|528501765|ref|XP_005157640|]
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histone-lysine N-methyltransferase 2A isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 4066-4219 7.94e-109

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: 343.93  E-value: 7.94e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4066 LPEKFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDA 4145
Cdd:cd19206     1 MPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528501765 4146 TIHGNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFLN 4219
Cdd:cd19206    81 TMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 2066-2178 5.11e-82

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: 265.33  E-value: 5.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2066 RQCALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSC 2145
Cdd:cd15693     1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 528501765 2146 TNNYHFMCARQQQCAFLEDKKVYCQHHKDLVKG 2178
Cdd:cd15693    81 TSNYHFMCSRAKNCVFLEDKKVYCQRHKDLIKG 113
Bromo_ALL-1 cd05493
Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and ...
 1841-1971 4.00e-52

Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and is often affected in chromosomal rearrangements that are linked to acute leukemias, such as acute lymphocytic leukemia (ALL). Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


:

Pssm-ID: 99925  Cd Length: 131  Bit Score: 180.71  E-value: 4.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 1841 VLTALFNSRTSTHLLRYRqavMKPPELNPETEESLPSRRSPEGPDPPV---LTEVSPPNDSPLDLESVEKKMDSGCYKSV 1917
Cdd:cd05493     1 ELEELLDSRTKSHLLRCG---PKPPALLPETEESLPGRKSPVTPEVLQgllSSEVKQEELPPLDLEAVGKKLEAGFYTSV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 1918 LEFSDDIVKIIQTAFNSDGGQLESRKANSMLKSFFIRQMERIFPWYKVKESKFW 1971
Cdd:cd05493    78 LDFSDDIVKIIQAALNSEGGQPEIKKANSMAKSFFIKLMESVFPWFNSEDPKLW 131
PHD1_KMT2A cd15588
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1627-1673 6.98e-33

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: 122.37  E-value: 6.98e-33
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 528501765 1627 VCFLCASSGNVEFVFCQVCCEPFHLFCLGEAERPHDEQWENWCCRRC 1673
Cdd:cd15588     1 VCFLCASSGHVEFVYCQVCCEPFHKFCLEEAERPLEDQLENWCCRRC 47
PHD2_KMT2A cd15590
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1675-1724 5.94e-32

PHD finger 2 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 second PHD finger.


:

Pssm-ID: 277065  Cd Length: 50  Bit Score: 120.13  E-value: 5.94e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKKRVWVCTKC 1724
Cdd:cd15590     1 FCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKRVWICTKC 50
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 3919-4002 2.09e-30

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: 116.63  E-value: 2.09e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765   3919 LIFEICSDDGFQIRCESIEEAWKSLTDKVQEARSNARLKALSFDGVNGLKMLGVVHDAVVFLLEQLYGARHCRNYRFRFH 3998
Cdd:smart00542    2 FRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWFRYH 81


                    ....
gi 528501765   3999 KPEE 4002
Cdd:smart00542   82 RSPL 85
PHD3_KMT2A cd15592
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1762-1818 1.24e-29

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: 113.54  E-value: 1.24e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1762 LCPLCNKGYDDDDCDSKMMKCKKCDRWVHAKCESLTDDMCELMSSLPENVVYTCTNC 1818
Cdd:cd15592     1 FCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCINC 57
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 1312-1359 7.20e-20

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


:

Pssm-ID: 366873  Cd Length: 48  Bit Score: 85.48  E-value: 7.20e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 528501765  1312 RKGRRSRRCGQCPGCQVPNDCGVCTNCLDKPKFGGRNIKKQCCKVRKC 1359
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2219-2266 6.88e-15

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: 71.38  E-value: 6.88e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528501765  2219 GSMTIDCLGMLTELS---DCERKLFPVGYQCSRVYWSTLDARKRCVYKCRI 2266
Cdd:pfam05964    1 GSLTVLSLGEIVPDRpafHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 3221-3709 7.42e-04

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 7.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3221 PLISETSERTMLALATEESEAGKSKKkTRTGSTVSSKSPQEGCADSQVPEGHMTPEHFIPPSVDGDHITSPGVAPVGETG 3300
Cdd:pfam03154   76 PLKSAKRQREKGASDTEEPERATAKK-SKTQEISRPNSPSEGEGESSDGRSVNDEGSSDPKDIDQDNRSTSPSIPSPQDN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3301 NQDMTRTSSTPVLPSSP-TLPLQNQKFIPATTVTSGPAPITSSAVQAAASQLKPGPEKLIvlnqhlqplyvlqTVPNGVM 3379
Cdd:pfam03154  155 ESDSDSSAQQQILQTQPpVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT-------------SQPPNQT 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3380 NPNAPVLTGLSGGISTSQSIFPAGSKGLVPVSHHPQihaftgTTQTGFQPVIPSTTSGLlIGVTSHDPQIGVTEAGHRHD 3459
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPP------PSQVSPQPLPQPSLHGQ-MPPMPHSLQTGPSHMQHPVP 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3460 HAP-NVAMVSSASTITPAPSMIPSGHGKKRLISRLQSPKSKKQARPKTQPtLAPSDvgpnMTLINLSPsqiaagiPAQTG 3538
Cdd:pfam03154  295 PQPfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP-LPPAP----LSMPHIKP-------PPTTP 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3539 LMELGTITATPHrkiPNIIKRPKQGVMylePTILPQP---MPISTTTQpgilGHDSSTHllPCTVSGLNTSQSvlnVVSV 3615
Cdd:pfam03154  363 IPQLPNPQSHKH---PPHLSGPSPFQM---NSNLPPPpalKPLSSLST----HHPPSAH--PPPLQLMPQSQQ---LPPP 427

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3616 PSSAPGNflgGSSVSLSAPGliSSTEITGSLSNLLIKA--NPHNLSLSEQPMVLHPGTP------MMSHLTNPAQTSIAS 3687
Cdd:pfam03154  428 PAQPPVL---TQSQSLPPPA--ASHPPTSGLHQVPSQSpfPQHPFVPGGPPPITPPSGPptstssAMPGIQPPSSASVSS 502

                          490       500
                   ....*....|....*....|....*....
gi 528501765  3688 SI-------CVFPPNQSITVPVNQQVEKE 3709
Cdd:pfam03154  503 SGpvpaavsCPLPPVQIKEEALDEAEEPE 531
 
Name Accession Description Interval E-value
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 4066-4219 7.94e-109

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: 343.93  E-value: 7.94e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4066 LPEKFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDA 4145
Cdd:cd19206     1 MPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528501765 4146 TIHGNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFLN 4219
Cdd:cd19206    81 TMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 2066-2178 5.11e-82

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: 265.33  E-value: 5.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2066 RQCALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSC 2145
Cdd:cd15693     1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 528501765 2146 TNNYHFMCARQQQCAFLEDKKVYCQHHKDLVKG 2178
Cdd:cd15693    81 TSNYHFMCSRAKNCVFLEDKKVYCQRHKDLIKG 113
Bromo_ALL-1 cd05493
Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and ...
 1841-1971 4.00e-52

Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and is often affected in chromosomal rearrangements that are linked to acute leukemias, such as acute lymphocytic leukemia (ALL). Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99925  Cd Length: 131  Bit Score: 180.71  E-value: 4.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 1841 VLTALFNSRTSTHLLRYRqavMKPPELNPETEESLPSRRSPEGPDPPV---LTEVSPPNDSPLDLESVEKKMDSGCYKSV 1917
Cdd:cd05493     1 ELEELLDSRTKSHLLRCG---PKPPALLPETEESLPGRKSPVTPEVLQgllSSEVKQEELPPLDLEAVGKKLEAGFYTSV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 1918 LEFSDDIVKIIQTAFNSDGGQLESRKANSMLKSFFIRQMERIFPWYKVKESKFW 1971
Cdd:cd05493    78 LDFSDDIVKIIQAALNSEGGQPEIKKANSMAKSFFIKLMESVFPWFNSEDPKLW 131
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 4081-4201 1.68e-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: 158.65  E-value: 1.68e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765   4081 VGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGI-GCYMFRIDDYEVVDATIHGNSARFINHSC 4159
Cdd:smart00317    3 LEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHSC 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528501765   4160 EPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEP 4201
Cdd:smart00317   83 EPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
4085-4216 8.34e-37

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 137.02  E-value: 8.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4085 RSAIHGRGLFCRKNIEPGEMVIEYSGNVIRsvlTDKREKYYDDKGIGC-YMFRIDDYEVVDATIHGNSARFINHSCEPNC 4163
Cdd:COG2940    12 PSPIHGRGVFATRDIPKGTLIGEYPGEVIT---WAEAERREPHKEPLHtYLFELDDDGVIDGALGGNPARFINHSCDPNC 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528501765 4164 YSRVVNvdgqKHIVIFATRKIYKGEELTYDYKFPIEEPgnKLPCNCgaKKCRK 4216
Cdd:COG2940    89 EADEED----GRIFIVALRDIAAGEELTYDYGLDYDEE--EYPCRC--PNCRG 133
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 4090-4195 4.47e-34

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: 128.41  E-value: 4.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  4090 GRGLFCRKNIEPGEMVIEYSGN-VIRSVLTDKREKYYDDKGI----GCYMFRIDDYE--VVDATI--HGNSARFINHSCE 4160
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDSeyCIDARAlyYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 528501765  4161 PNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYK 4195
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
PHD1_KMT2A cd15588
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1627-1673 6.98e-33

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: 122.37  E-value: 6.98e-33
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 528501765 1627 VCFLCASSGNVEFVFCQVCCEPFHLFCLGEAERPHDEQWENWCCRRC 1673
Cdd:cd15588     1 VCFLCASSGHVEFVYCQVCCEPFHKFCLEEAERPLEDQLENWCCRRC 47
PHD2_KMT2A cd15590
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1675-1724 5.94e-32

PHD finger 2 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 second PHD finger.


Pssm-ID: 277065  Cd Length: 50  Bit Score: 120.13  E-value: 5.94e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKKRVWVCTKC 1724
Cdd:cd15590     1 FCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKRVWICTKC 50
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 3919-4002 2.09e-30

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: 116.63  E-value: 2.09e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765   3919 LIFEICSDDGFQIRCESIEEAWKSLTDKVQEARSNARLKALSFDGVNGLKMLGVVHDAVVFLLEQLYGARHCRNYRFRFH 3998
Cdd:smart00542    2 FRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWFRYH 81


                    ....
gi 528501765   3999 KPEE 4002
Cdd:smart00542   82 RSPL 85
PHD3_KMT2A cd15592
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1762-1818 1.24e-29

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: 113.54  E-value: 1.24e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1762 LCPLCNKGYDDDDCDSKMMKCKKCDRWVHAKCESLTDDMCELMSSLPENVVYTCTNC 1818
Cdd:cd15592     1 FCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCINC 57
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 3914-3998 3.67e-24

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: 98.83  E-value: 3.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3914 KPKkgLIFEICSDDGFQIRCESIEEAWKSLTDKVQEARSNARLKALSFDGVNGLKMLGVVHDAVVFLLEQLYGARHCRNY 3993
Cdd:pfam05965    1 GPL--FRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78


                   ....*
gi 528501765  3994 RFRFH 3998
Cdd:pfam05965   79 KFRYG 83
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 1312-1359 7.20e-20

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 85.48  E-value: 7.20e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 528501765  1312 RKGRRSRRCGQCPGCQVPNDCGVCTNCLDKPKFGGRNIKKQCCKVRKC 1359
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 2095-2172 1.01e-16

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: 77.75  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  2095 HVNCALWSAEVY--EDVDGA--LKNVHMAVSRGKQLQCKNCHKP-GATVSCCMTSCTNNYHFMCARQQQCAFLEDK---- 2165
Cdd:pfam13771    1 HVVCALWSPELVqrGNDSMGfpIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDEdngt 80


                   ....*...
gi 528501765  2166 -KVYCQHH 2172
Cdd:pfam13771   81 fKSYCKKH 88
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2219-2266 6.88e-15

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: 71.38  E-value: 6.88e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528501765  2219 GSMTIDCLGMLTELS---DCERKLFPVGYQCSRVYWSTLDARKRCVYKCRI 2266
Cdd:pfam05964    1 GSLTVLSLGEIVPDRpafHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
 2225-2267 8.12e-13

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: 65.38  E-value: 8.12e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 528501765   2225 CLGMLTELSDCERKLFPVGYQCSRVYWSTLDARKRCVYKCRIL 2267
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVID 43
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1675-1724 2.20e-10

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: 58.38  E-value: 2.20e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 528501765   1675 FCHVCGRKYqKTKQLLECDKCRNSYHPECLGPnhPTRPTKKKRVWVCTKC 1724
Cdd:smart00249    1 YCSVCGKPD-DGGELLQCDGCDRWYHQTCLGP--PLLEEEPDGKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1627-1676 1.04e-09

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: 56.73  E-value: 1.04e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528501765  1627 VCFLCASSGN-VEFVFCQVCCEPFHLFCLGEAERPHDEQWENWCCRRCRFC 1676
Cdd:pfam00628    1 YCAVCGKSDDgGELVQCDGCDDWFHLACLGPPLDPAEIPSGEWLCPECKPK 51
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1675-1727 1.18e-09

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: 56.35  E-value: 1.18e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 528501765  1675 FCHVCGRkYQKTKQLLECDKCRNSYHPECLGPNhPTRPTKKKRVWVCTKCVRC 1727
Cdd:pfam00628    1 YCAVCGK-SDDGGELVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1763-1818 6.74e-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: 51.44  E-value: 6.74e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 528501765   1763 CPLCNKGYDDDDcdskMMKCKKCDRWVHAKCESLTDDmcelmsSLPENVVYTCTNC 1818
Cdd:smart00249    2 CSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLL------EEEPDGKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1763-1821 9.19e-08

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 51.34  E-value: 9.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 528501765  1763 CPLCNKgyddDDCDSKMMKCKKCDRWVHAKCESLTDDMCELMSSlpenvVYTCTNCTES 1821
Cdd:pfam00628    2 CAVCGK----SDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1627-1673 3.36e-07

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 49.52  E-value: 3.36e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 528501765   1627 VCFLCASSGN-VEFVFCQVCCEPFHLFCLGEAERPHDEQwENWCCRRC 1673
Cdd:smart00249    1 YCSVCGKPDDgGELLQCDGCDRWYHQTCLGPPLLEEEPD-GKWYCPKC 47
BROMO smart00297
bromo domain;
1899-1959 1.29e-06

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 49.58  E-value: 1.29e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501765   1899 PLDLESVEKKMDSGCYKSVLEFSDDIVKIIQTAFNSDGGQLESRKANSMLKSFFIRQMERI 1959
Cdd:smart00297   47 PMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
2066-2168 2.54e-04

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 47.28  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2066 RQCALCLNY-GDEKTNDCGRllyighneWAHVNCALWSAEVY-------EDVDGaLKNVhmAVSRGKqLQCKNCHKPGAT 2137
Cdd:COG5141   248 RCCSFCPSSdGAFKQTSDGR--------WGHVICAMFNPELSfghllskDPIDN-IASV--SSSRWK-LGCLICKEFGGT 315

                          90       100       110
                  ....*....|....*....|....*....|..
gi 528501765 2138 -VSCCMTSCTNNYHFMCARqQQCAFleDKKVY 2168
Cdd:COG5141   316 cIQCSYFNCTRAYHVTCAR-RAGYF--DLNIY 344
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 3221-3709 7.42e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 7.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3221 PLISETSERTMLALATEESEAGKSKKkTRTGSTVSSKSPQEGCADSQVPEGHMTPEHFIPPSVDGDHITSPGVAPVGETG 3300
Cdd:pfam03154   76 PLKSAKRQREKGASDTEEPERATAKK-SKTQEISRPNSPSEGEGESSDGRSVNDEGSSDPKDIDQDNRSTSPSIPSPQDN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3301 NQDMTRTSSTPVLPSSP-TLPLQNQKFIPATTVTSGPAPITSSAVQAAASQLKPGPEKLIvlnqhlqplyvlqTVPNGVM 3379
Cdd:pfam03154  155 ESDSDSSAQQQILQTQPpVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT-------------SQPPNQT 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3380 NPNAPVLTGLSGGISTSQSIFPAGSKGLVPVSHHPQihaftgTTQTGFQPVIPSTTSGLlIGVTSHDPQIGVTEAGHRHD 3459
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPP------PSQVSPQPLPQPSLHGQ-MPPMPHSLQTGPSHMQHPVP 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3460 HAP-NVAMVSSASTITPAPSMIPSGHGKKRLISRLQSPKSKKQARPKTQPtLAPSDvgpnMTLINLSPsqiaagiPAQTG 3538
Cdd:pfam03154  295 PQPfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP-LPPAP----LSMPHIKP-------PPTTP 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3539 LMELGTITATPHrkiPNIIKRPKQGVMylePTILPQP---MPISTTTQpgilGHDSSTHllPCTVSGLNTSQSvlnVVSV 3615
Cdd:pfam03154  363 IPQLPNPQSHKH---PPHLSGPSPFQM---NSNLPPPpalKPLSSLST----HHPPSAH--PPPLQLMPQSQQ---LPPP 427

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3616 PSSAPGNflgGSSVSLSAPGliSSTEITGSLSNLLIKA--NPHNLSLSEQPMVLHPGTP------MMSHLTNPAQTSIAS 3687
Cdd:pfam03154  428 PAQPPVL---TQSQSLPPPA--ASHPPTSGLHQVPSQSpfPQHPFVPGGPPPITPPSGPptstssAMPGIQPPSSASVSS 502

                          490       500
                   ....*....|....*....|....*....
gi 528501765  3688 SI-------CVFPPNQSITVPVNQQVEKE 3709
Cdd:pfam03154  503 SGpvpaavsCPLPPVQIKEEALDEAEEPE 531
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 2128-2172 1.03e-03

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 39.50  E-value: 1.03e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 528501765   2128 CKNCHKPGATVSCCMtsCTNNYHFMCARQQQCAFLEDKKVYCQHH 2172
Cdd:smart00249    5 CGKPDDGGELLQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
 
Name Accession Description Interval E-value
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 4066-4219 7.94e-109

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: 343.93  E-value: 7.94e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4066 LPEKFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDA 4145
Cdd:cd19206     1 MPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528501765 4146 TIHGNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFLN 4219
Cdd:cd19206    81 TMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 4069-4219 6.08e-105

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: 332.82  E-value: 6.08e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDATIH 4148
Cdd:cd19170     4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501765 4149 GNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEpgNKLPCNCGAKKCRKFLN 4219
Cdd:cd19170    84 GNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIED--VKIPCTCGSKKCRKYLN 152
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 4066-4215 2.67e-86

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: 279.10  E-value: 2.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4066 LPEKFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGI-GCYMFRIDDYEVVD 4144
Cdd:cd10518     1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGgGTYMFRIDEDLVID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501765 4145 ATIHGNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEpGNKLPCNCGAKKCR 4215
Cdd:cd10518    81 ATKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIED-EEKIPCLCGAPNCR 150
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 4069-4219 1.23e-85

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: 277.67  E-value: 1.23e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDATIH 4148
Cdd:cd19207     4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501765 4149 GNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFLN 4219
Cdd:cd19207    84 GNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 154
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 2066-2178 5.11e-82

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: 265.33  E-value: 5.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2066 RQCALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSC 2145
Cdd:cd15693     1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 528501765 2146 TNNYHFMCARQQQCAFLEDKKVYCQHHKDLVKG 2178
Cdd:cd15693    81 TSNYHFMCSRAKNCVFLEDKKVYCQRHKDLIKG 113
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 2068-2172 4.55e-64

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: 213.81  E-value: 4.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15664     1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                          90       100
                  ....*....|....*....|....*
gi 528501765 2148 NYHFMCARQQQCAFLEDKKVYCQHH 2172
Cdd:cd15664    81 NYHFMCARKAECVFQDDKKVFCPAH 105
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 4069-4215 6.79e-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: 214.89  E-value: 6.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKkASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIG-CYMFRIDDYEVVDATI 4147
Cdd:cd19169     4 KFNQLK-FRKKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGsSYLFRVDDDTIIDATK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 4148 HGNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEpgNKLPCNCGAKKCR 4215
Cdd:cd19169    83 CGNLARFINHSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIED--EKIPCLCGAPQCR 148
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 4069-4218 1.46e-61

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: 208.44  E-value: 1.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDATIH 4148
Cdd:cd19171     4 QYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDATMT 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4149 GNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFL 4218
Cdd:cd19171    84 GGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 4069-4215 2.48e-56

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: 193.41  E-value: 2.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKKaSRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIG-CYMFRIDDYEVVDATI 4147
Cdd:cd20072     4 RFNQLKK-RKKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDATK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 4148 HGNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEpgNKLPCNCGAKKCR 4215
Cdd:cd20072    83 KGNIARFINHCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREE--DKIPCLCGAPNCR 148
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 2068-2172 4.13e-55

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: 187.94  E-value: 4.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15694     1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                          90       100
                  ....*....|....*....|....*
gi 528501765 2148 NYHFMCARQQQCAFLEDKKVYCQHH 2172
Cdd:cd15694    81 NFHFMCARASRCCFQDDKKVFCQKH 105
Bromo_ALL-1 cd05493
Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and ...
 1841-1971 4.00e-52

Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and is often affected in chromosomal rearrangements that are linked to acute leukemias, such as acute lymphocytic leukemia (ALL). Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99925  Cd Length: 131  Bit Score: 180.71  E-value: 4.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 1841 VLTALFNSRTSTHLLRYRqavMKPPELNPETEESLPSRRSPEGPDPPV---LTEVSPPNDSPLDLESVEKKMDSGCYKSV 1917
Cdd:cd05493     1 ELEELLDSRTKSHLLRCG---PKPPALLPETEESLPGRKSPVTPEVLQgllSSEVKQEELPPLDLEAVGKKLEAGFYTSV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 1918 LEFSDDIVKIIQTAFNSDGGQLESRKANSMLKSFFIRQMERIFPWYKVKESKFW 1971
Cdd:cd05493    78 LDFSDDIVKIIQAALNSEGGQPEIKKANSMAKSFFIKLMESVFPWFNSEDPKLW 131
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 4069-4219 6.76e-46

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: 163.69  E-value: 6.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKkASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGC-YMFRIDDYEVVDATI 4147
Cdd:cd19205     5 KFNQLK-FRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDATK 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528501765 4148 HGNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEpgNKLPCNCGAKKCRKFLN 4219
Cdd:cd19205    84 CGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIED--VKIPCLCGSENCRGTLN 153
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 4085-4219 2.17e-45

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: 162.12  E-value: 2.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4085 RSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGC-YMFRIDDYEVVDATIHGNSARFINHSCEPNC 4163
Cdd:cd19204    20 RSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLARFINHCCTPNC 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528501765 4164 YSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEpgNKLPCNCGAKKCRKFLN 4219
Cdd:cd19204   100 YAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIED--NKIPCLCGTENCRGTLN 153
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
 4069-4218 4.00e-45

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: 161.72  E-value: 4.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDATIH 4148
Cdd:cd19208     5 QYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVIDATLT 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4149 GNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFL 4218
Cdd:cd19208    85 GGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 154
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 4069-4218 1.15e-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: 160.25  E-value: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMFRIDDYEVVDATIH 4148
Cdd:cd19209     6 QYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLT 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4149 GNSARFINHSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFL 4218
Cdd:cd19209    86 GGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 4081-4201 1.68e-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: 158.65  E-value: 1.68e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765   4081 VGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGI-GCYMFRIDDYEVVDATIHGNSARFINHSC 4159
Cdd:smart00317    3 LEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHSC 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528501765   4160 EPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEP 4201
Cdd:smart00317   83 EPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 2068-2172 7.29e-42

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: 150.14  E-value: 7.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15666     1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                          90       100
                  ....*....|....*....|....*
gi 528501765 2148 NYHFMCARQQQCAFLEDKKVYCQHH 2172
Cdd:cd15666    81 VYHLPCAIKDGCMFFKDKTMLCPSH 105
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 4090-4215 7.32e-39

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: 142.78  E-value: 7.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4090 GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKR-EKYYDDKGIGCYMFRIDDYEVVDATIHGNSARFINHSCEPNCYSRVV 4168
Cdd:cd10531    11 GWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERlDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFINHSCEPNCETQKW 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 528501765 4169 NVDGQKHIVIFATRKIYKGEELTYDYKFpIEEPGNKLPCNCGAKKCR 4215
Cdd:cd10531    91 IVNGEYRIGIFALRDIPAGEELTFDYNF-VNYNEAKQVCLCGAQNCR 136
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
4085-4216 8.34e-37

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 137.02  E-value: 8.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4085 RSAIHGRGLFCRKNIEPGEMVIEYSGNVIRsvlTDKREKYYDDKGIGC-YMFRIDDYEVVDATIHGNSARFINHSCEPNC 4163
Cdd:COG2940    12 PSPIHGRGVFATRDIPKGTLIGEYPGEVIT---WAEAERREPHKEPLHtYLFELDDDGVIDGALGGNPARFINHSCDPNC 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528501765 4164 YSRVVNvdgqKHIVIFATRKIYKGEELTYDYKFPIEEPgnKLPCNCgaKKCRK 4216
Cdd:COG2940    89 EADEED----GRIFIVALRDIAAGEELTYDYGLDYDEE--EYPCRC--PNCRG 133
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 4090-4218 7.73e-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: 134.47  E-value: 7.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4090 GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKG-IGCYMFRIDDYEVVDATIHGNSARFINHSCEPNCYSRVV 4168
Cdd:cd19175    11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGeKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 4169 NVDGQKHIVIFATRKIYKGEELTYDYKFpiEEPGNKLPCNCGAKKCRKFL 4218
Cdd:cd19175    91 QVDGETRIGVFAIRDIKKGEELTYDYQF--VQFGADQDCHCGSKNCRGKL 138
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 4081-4218 1.86e-35

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: 133.48  E-value: 1.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4081 VGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGCYMF-RIDDYEVVDATIHGNSARFINHSC 4159
Cdd:cd19172     4 VEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFmALKSDEIIDATKKGNLSRFINHSC 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4160 EPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFpiEEPGNK-LPCNCGAKKCRKFL 4218
Cdd:cd19172    84 EPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQF--ERYGKEaQKCYCGSPNCRGYI 141
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 4081-4194 3.88e-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: 3.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4081 VGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGcYMFRIDDYEVVDATIHGNSARFINHSCE 4160
Cdd:cd10519     3 LLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSN 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 528501765 4161 PNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd10519    82 PNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDY 115
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 4090-4195 4.47e-34

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: 128.41  E-value: 4.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  4090 GRGLFCRKNIEPGEMVIEYSGN-VIRSVLTDKREKYYDDKGI----GCYMFRIDDYE--VVDATI--HGNSARFINHSCE 4160
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDSeyCIDARAlyYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 528501765  4161 PNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYK 4195
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 4083-4219 4.50e-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: 129.33  E-value: 4.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKR--EKYYDDKGIgcYMFRIDDYEVVDATIHGNSARFINHSCE 4160
Cdd:cd19174     4 RFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRmiEQYHNHSHH--YCLNLDSGMVIDGYRMGNEARFVNHSCD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528501765 4161 PNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNCGAKKCRKFLN 4219
Cdd:cd19174    82 PNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG 140
PHD1_KMT2A cd15588
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1627-1673 6.98e-33

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: 122.37  E-value: 6.98e-33
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 528501765 1627 VCFLCASSGNVEFVFCQVCCEPFHLFCLGEAERPHDEQWENWCCRRC 1673
Cdd:cd15588     1 VCFLCASSGHVEFVYCQVCCEPFHKFCLEEAERPLEDQLENWCCRRC 47
PHD2_KMT2A cd15590
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1675-1724 5.94e-32

PHD finger 2 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 second PHD finger.


Pssm-ID: 277065  Cd Length: 50  Bit Score: 120.13  E-value: 5.94e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKKRVWVCTKC 1724
Cdd:cd15590     1 FCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKRVWICTKC 50
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 2068-2172 7.81e-31

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: 118.61  E-value: 7.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15697     1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                          90       100
                  ....*....|....*....|....*
gi 528501765 2148 NYHFMCARQQQCAFLEDKKVYCQHH 2172
Cdd:cd15697    81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 3919-4002 2.09e-30

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: 116.63  E-value: 2.09e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765   3919 LIFEICSDDGFQIRCESIEEAWKSLTDKVQEARSNARLKALSFDGVNGLKMLGVVHDAVVFLLEQLYGARHCRNYRFRFH 3998
Cdd:smart00542    2 FRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWFRYH 81


                    ....
gi 528501765   3999 KPEE 4002
Cdd:smart00542   82 RSPL 85
PHD3_KMT2A cd15592
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 1762-1818 1.24e-29

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: 113.54  E-value: 1.24e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1762 LCPLCNKGYDDDDCDSKMMKCKKCDRWVHAKCESLTDDMCELMSSLPENVVYTCTNC 1818
Cdd:cd15592     1 FCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCINC 57
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 4090-4218 3.00e-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: 3.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4090 GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIgCYMFRIDDYE-----VVDATIHGNSARFINHSCEPN-- 4162
Cdd:cd10542    99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDYNDddceyTVDAAYYGNISHFINHSCDPNla 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 4163 CYSRVVNV-DGQK-HIVIFATRKIYKGEELTYDYKF-----PIEEPGNK-----LPCNCGAKKCRKFL 4218
Cdd:cd10542   178 VYAVWINHlDPRLpRIAFFAKRDIKAGEELTFDYLMtgtggSSESTIPKpkdvrVPCLCGSKNCRKYL 245
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 4083-4218 8.16e-29

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: 114.33  E-value: 8.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGI-GCYMFRIDDYEVVDATIHGNSARFINHSCEP 4161
Cdd:cd19173     6 PFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNItNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 4162 NCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFpiEEPGN-KLPCNCGAKKCRKFL 4218
Cdd:cd19173    86 NCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNL--DCLGNeKKVCRCGAPNCSGFL 141
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 2068-2173 1.09e-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: 112.84  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15698     1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                          90       100
                  ....*....|....*....|....*.
gi 528501765 2148 NYHFMCARQQQCAFLEDKKVYCQHHK 2173
Cdd:cd15698    81 VYHFACAIRAKCMFFKDKTMLCPMHK 106
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 4083-4194 1.11e-27

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: 114.01  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGiGCYMFRIDDYE---------VVDATIHGNSAR 4153
Cdd:cd10538    93 VFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSG-GSYLFDLDEFSdsdgdgeelCVDATFCGNVSR 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528501765 4154 FINHSCEPNCYSRVVNVDGQKH----IVIFATRKIYKGEELTYDY 4194
Cdd:cd10538   172 FINHSCDPNLFPFNVVIDHDDLryprIALFATRDILPGEELTFDY 216
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 4090-4194 2.12e-27

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


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 109.74  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4090 GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKgigCYMFRIDDYE-VVDATIHGNSARFINHSCEPNCYSRVV 4168
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDP---LYPFDLNGDIlVIDAGKKGNLTRFINHSDQPNLELIVR 90

                          90       100
                  ....*....|....*....|....*.
gi 528501765 4169 NVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd10522    91 TLKGEQHIGFVAIRDIKPGEELFISY 116
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 2068-2172 3.76e-27

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: 108.44  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKTNdCGRLLYIGHNEWAHVNCALWSAEVYEDVDGALK--NVHMAVSRGKQLQCKNCHKP-GATVSCCMTS 2144
Cdd:cd15571     1 CALCPRSGGALKG-GGALKTTSDGLWVHVVCALWSPEVYFDDGTLLEveGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 528501765 2145 CTNNYHFMCARQQQCAFL-----EDKKVYCQHH 2172
Cdd:cd15571    80 CPRSFHVSCAIRAGCLFEfedgpGNFVVYCPKH 112
PHD3_KMT2A_like cd15508
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 1762-1818 9.11e-27

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: 105.22  E-value: 9.11e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1762 LCPLCNKGYDDDDCDSKMMKCKKCDRWVHAKCESLTDDMCELMSSLPENVVYTCTNC 1818
Cdd:cd15508     1 YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC 57
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 4071-4194 3.73e-25

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: 103.81  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4071 RQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKRE-KYYDDKGIGCYMFRID----DYeVVDA 4145
Cdd:cd10528     9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREaLYAKDPSTGCYMYYFQykgkTY-CVDA 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 4146 TI----HGnsaRFINHSC-EPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd10528    88 TKesgrLG---RLINHSKkKPNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 3914-3998 3.67e-24

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: 98.83  E-value: 3.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3914 KPKkgLIFEICSDDGFQIRCESIEEAWKSLTDKVQEARSNARLKALSFDGVNGLKMLGVVHDAVVFLLEQLYGARHCRNY 3993
Cdd:pfam05965    1 GPL--FRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78


                   ....*
gi 528501765  3994 RFRFH 3998
Cdd:pfam05965   79 KFRYG 83
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 4081-4218 4.56e-24

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: 100.77  E-value: 4.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4081 VGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGI-GCYMFRIDDYEVVDATIHGNSARFINHSC 4159
Cdd:cd19210     4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItNFYMLTLDKDRIIDAGPKGNYARFMNHCC 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4160 EPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKfpIEEPGN-KLPCNCGAKKCRKFL 4218
Cdd:cd19210    84 QPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYN--LECLGNgKTVCKCGAPNCSGFL 141
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 4086-4196 6.87e-24

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: 99.60  E-value: 6.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4086 SAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDdKGIGCYMFRIDDYEVVDATIHGNSARFINHSCEPNCYS 4165
Cdd:cd19218    11 SDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 528501765 4166 RVVNVDGQKHIVIFATRKIYKGEELTYDYKF 4196
Cdd:cd19218    90 KVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120
PHD2_KMT2A_like cd15507
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 1675-1724 1.15e-23

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: 96.38  E-value: 1.15e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKKRVWVCTKC 1724
Cdd:cd15507     1 FCHVCGRKGQAQKQLLECEKCQRGYHVDCLGPSYPTKPTRKKKTWICSKC 50
PHD3_KMT2B cd15593
PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
 1763-1818 2.09e-23

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: 95.69  E-value: 2.09e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528501765 1763 CPLCNKGYDDDDCDSKMMKCKKCDRWVHAKCESLTDDMCELMSSLPENVVYTCTNC 1818
Cdd:cd15593     2 CPICLKCYEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSLPDSVVYSCAPC 57
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 4086-4196 3.62e-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: 98.22  E-value: 3.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4086 SAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDdKGIGCYMFRIDDYEVVDATIHGNSARFINHSCEPNCYS 4165
Cdd:cd19217    13 SDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 528501765 4166 RVVNVDGQKHIVIFATRKIYKGEELTYDYKF 4196
Cdd:cd19217    92 KVVMVNGDHRIGIFAKRAIQQGEELFFDYRY 122
PHD2_KMT2B cd15591
PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
 1675-1724 5.58e-23

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: 94.23  E-value: 5.58e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKKRVWVCTKC 1724
Cdd:cd15591     1 FCHVCGRKNKESKPLLECERCRNCYHPACLGPNYPKPANRKKRPWICSAC 50
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 4083-4218 8.53e-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: 97.37  E-value: 8.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIG-CYMFRIDDYEVVDATIHGNSARFINHSCEP 4161
Cdd:cd19211     6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDIThFYMLTIDKDRIIDAGPKGNYSRFMNHSCQP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 4162 NCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKfpIEEPGN-KLPCNCGAKKCRKFL 4218
Cdd:cd19211    86 NCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYN--LDCLGNeKTVCRCGAPNCSGFL 141
PHD1_KMT2A_like cd15506
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 1627-1673 9.06e-23

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: 93.58  E-value: 9.06e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 528501765 1627 VCFLCASSGNVEFVFCQVCCEPFHLFCLGEAERPHDEQWENWCCRRC 1673
Cdd:cd15506     1 LCFLCGSAGLNELLYCSVCCEPYHTFCLEEAERPLNINKDNWCCRRC 47
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 4083-4218 6.53e-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: 98.14  E-value: 6.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVI------RSVLTDK----------REKYYDDKGIGCYmfriddyevVDAT 4146
Cdd:cd10544    94 VFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIgfeearRRTKSQTkgdmnyiivlREHLSSGKVLETF---------VDPT 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4147 IHGNSARFINHSCEPNCYSRVVNVDGQ-KHIVIFATRKIYKGEELTYDY------------KFPIEEPGNKLPCNCGAKK 4213
Cdd:cd10544   165 YIGNIGRFLNHSCEPNLFMVPVRVDSMvPKLALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSRKPCLCGAEN 244


                  ....*
gi 528501765 4214 CRKFL 4218
Cdd:cd10544   245 CRGFL 249
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 4083-4218 9.00e-22

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: 98.03  E-value: 9.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIgCYMFRIDDYE-------VVDATIHGNSARFI 4155
Cdd:cd20073    97 IFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDNVGV-TYLFDLDLFEdqvdeyyTVDAQYCGDVTRFI 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4156 NHSCEPN--CYSRVVNVDGQK--HIVIFATRKIYKGEELTYDYK-----FPIEEPGN-----------KLPCNCGAKKCR 4215
Cdd:cd20073   176 NHSCDPNlaIYSVLRDKSDSKiyDLAFFAIKDIPALEELTFDYSgrnnfDQLGFIGNrsnskyinlknKRPCYCGSANCR 255


                  ...
gi 528501765 4216 KFL 4218
Cdd:cd20073   256 GWL 258
PHD1_KMT2B cd15589
PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
 1627-1673 1.03e-21

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: 90.69  E-value: 1.03e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 528501765 1627 VCFLCASSGNVEFVFCQVCCEPFHLFCLGEAERPHDEQWENWCCRRC 1673
Cdd:cd15589     1 VCLLCASKGQHELLFCQVCCEPFHRFCLEESERPLPEQEENWCCRRC 47
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 4091-4194 4.12e-21

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: 91.95  E-value: 4.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4091 RGLFCRKNIEPGEMVIEYSGNVirSVLTDKREKYYDDKGIGCYMFRIDDYE----VVDATIHGNSARFINHSCEPNCYSR 4166
Cdd:cd10529    17 KGLVATEDISPGEPILEYKGEV--SLRSEFKEDNGFFKRPSPFVFFYDGFEglplCVDARKYGNEARFIRRSCRPNAELR 94

                          90       100       110
                  ....*....|....*....|....*....|.
gi 528501765 4167 VVNV-DGQKHIVIFATRKIYKGEELT--YDY 4194
Cdd:cd10529    95 HVVVsNGELRLFIFALKDIRKGTEITipFDY 125
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 4090-4218 5.70e-20

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: 89.21  E-value: 5.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4090 GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGI-GCYMFRIDDYEVVDATIHGNSARFINHSCEPNCYSRVV 4168
Cdd:cd19212    13 GWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVtNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQKW 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501765 4169 NVDGQKHIVIFATRKIYKGEELTYDYKfpIEEPGN-KLPCNCGAKKCRKFL 4218
Cdd:cd19212    93 TVNGDVRVGLFALCDIPAGMELTFNYN--LDCLGNgRTECHCGADNCSGFL 141
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 1312-1359 7.20e-20

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 85.48  E-value: 7.20e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 528501765  1312 RKGRRSRRCGQCPGCQVPNDCGVCTNCLDKPKFGGRNIKKQCCKVRKC 1359
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 4071-4215 9.00e-20

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: 91.25  E-value: 9.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4071 RQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREkyyDDKgigcYMFRIDDYEV----VDAT 4146
Cdd:cd10543    83 RVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRE---DDS----YLFDLDNKDGetycIDAR 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501765 4147 IHGNSARFINHSCEPNCYSRVVNVDGQK----HIVIFATRKIYKGEELTYDY--KFPIEEpGNKLPCNCGAKKCR 4215
Cdd:cd10543   156 RYGNISRFINHLCEPNLIPVRVFVEHQDlrfpRIAFFASRDIKAGEELGFDYgeKFWRIK-GKYFTCRCGSPKCK 229
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
 2068-2172 1.60e-19

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: 86.68  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNygDEKTNDCGRLLYIGHNEWAHVNCALWSAEVYEDVDGA--------LKNVHMAVSRGKQLQCKNCHKPGATVS 2139
Cdd:cd15673     1 CGFCKS--GEENKETGGKLASGEKIAAHHNCMLFSSGLVQYVSPNendfggfdIEDVKKEIKRGRKLKCNLCKKTGATIG 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 528501765 2140 CCMTSCTNNYHFMCARQQQCAFLEDK-----KVYCQHH 2172
Cdd:cd15673    79 CDVKQCKKTYHYHCAKKDDAKIIERNsqgiyRVYCKNH 116
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 4071-4218 2.41e-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: 90.34  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4071 RQLKKASRDAVGVYRSAiHGRGLFCR--KNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIgCYMFRID---DYEVVDA 4145
Cdd:cd10532    76 RVVQKGTQYSLCIFRTS-NGRGWGVKtlQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGI-TYLFDLDyesDEFTVDA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4146 TIHGNSARFINHSCEPNCYSRVVNVDGQK----HIVIFATRKIYKGEELTYDYKF------PIEEPGN-------KLPCN 4208
Cdd:cd10532   154 ARYGNVSHFVNHSCDPNLQVFNVFIDNLDtrlpRIALFSTRTIKAGEELTFDYQMkgsgdlSSDSIDNspakkrvRTVCK 233

                         170
                  ....*....|
gi 528501765 4209 CGAKKCRKFL 4218
Cdd:cd10532   234 CGAVTCRGYL 243
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 4083-4194 3.96e-19

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: 84.22  E-value: 3.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAI--HGRGLFCRKNIEPGEMVIEysgnvirsvltdkrekyyddkgigcymfriddyevvdatihgnsARFINHSCE 4160
Cdd:cd08161     2 IRPSTIpgAGFGLFATRDIPKGEVIGL--------------------------------------------ARFINHSCE 37

                          90       100       110
                  ....*....|....*....|....*....|....
gi 528501765 4161 PNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd08161    38 PNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 4071-4218 7.34e-19

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: 89.57  E-value: 7.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4071 RQLKKASRDAVGVYRSAiHGRGLFCR--KNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIgCYMFRID---DYEVVDA 4145
Cdd:cd10525    78 RVVQKGIQYDLCIFRTD-NGRGWGVRtlEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA-TYLFDLDyveDVYTVDA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4146 TIHGNSARFINHSCEPNCYSRVVNVDGQKH----IVIFATRKIYKGEELTYDYKFPIEE-----------------PGN- 4203
Cdd:cd10525   156 AYYGNISHFVNHSCDPNLQVYNVFIDNLDErlprIALFATRTIRAGEELTFDYNMQVDPvdaestkmdsnfglaglPGSp 235

                         170
                  ....*....|....*....
gi 528501765 4204 ----KLPCNCGAKKCRKFL 4218
Cdd:cd10525   236 kkrvRIECKCGVRSCRKYL 254
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
 4080-4194 9.02e-19

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: 84.93  E-value: 9.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4080 AVGVYRSAIH-GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGiGCYMFRIDDYEVVDATIHGNSARFINHS 4158
Cdd:cd19168     2 AVVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVS-YLYLFEEQEGIWVDAAIYGNLSRYINHA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528501765 4159 CEP----NCYSRVVNVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd19168    81 TDKvktgNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 4083-4218 2.29e-18

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: 88.89  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKgigcYMFRID----------DYE--------VVD 4144
Cdd:cd10517   133 VFKTEKKGWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYGDE----YFAELDyievveklkeGYEsdveehcyIID 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501765 4145 ATIHGNSARFINHSCEPNCYSRVVNVDGQK----HIVIFATRKIYKGEELTYDYKFPIEE-PGNKLPCNCGAKKCRKFL 4218
Cdd:cd10517   209 AKSEGNLGRYLNHSCSPNLFVQNVFVDTHDlrfpWVAFFASRYIRAGTELTWDYNYEVGSvPGKVLYCYCGSSNCRGRL 287
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 2093-2172 3.22e-18

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: 82.74  E-value: 3.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2093 WAHVNCALWSAEVYEdVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTNNYHFMCARQQQCAFLEDK-KVYCQH 2171
Cdd:cd15668    24 WVHEDCAVWAPGVYL-VGGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENfSLLCPK 102


                  .
gi 528501765 2172 H 2172
Cdd:cd15668   103 H 103
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 4071-4215 5.99e-17

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: 83.06  E-value: 5.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4071 RQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREkyyDDKgigcYMFRID--DYEV--VDAT 4146
Cdd:cd10535    83 RVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE---EDS----YLFDLDnkDGEVycIDAR 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501765 4147 IHGNSARFINHSCEPNCYSRVVNVDGQK----HIVIFATRKIYKGEELTYDY--KFpIEEPGNKLPCNCGAKKCR 4215
Cdd:cd10535   156 FYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYgeRF-WDIKGKLFSCRCGSPKCR 229
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 2095-2172 1.01e-16

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: 77.75  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  2095 HVNCALWSAEVY--EDVDGA--LKNVHMAVSRGKQLQCKNCHKP-GATVSCCMTSCTNNYHFMCARQQQCAFLEDK---- 2165
Cdd:pfam13771    1 HVVCALWSPELVqrGNDSMGfpIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDEdngt 80


                   ....*...
gi 528501765  2166 -KVYCQHH 2172
Cdd:pfam13771   81 fKSYCKKH 88
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 4069-4215 1.26e-16

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: 82.37  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4069 KFRQLKKASRDAVGVYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREkyyDDKgigcYMFRID--DYEV--VD 4144
Cdd:cd10533    81 KNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE---DDS----YLFDLDnkDGEVycID 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528501765 4145 ATIHGNSARFINHSCEPNCYSRVVNVDGQK----HIVIFATRKIYKGEELTYDYKFPIEEPGNK-LPCNCGAKKCR 4215
Cdd:cd10533   154 ARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 229
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 2068-2172 1.36e-16

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: 78.45  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKtNDCGRLLYIgHNEWAHVNCALWS------AEVYEDVDGAL-KNVHMAVSRGKQLQCKNCHKPGATVSC 2140
Cdd:cd15669     1 CVLCGRSDDDP-DKYGEKLQK-DGICAHYFCLLFSsglpqrGEDNEGIYGFLpEDIRKEVRRASRLRCFYCKKKGASIGC 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 528501765 2141 CMTSCTNNYHFMCARQQQCA--FLEDKKVYCQHH 2172
Cdd:cd15669    79 AVKGCRRSFHFPCGLENGCVtqFFGEYRSFCWEH 112
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 2068-2172 1.88e-16

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: 76.97  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALClnygdektnDCGRLlyighneWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15665     1 CALC---------NLGEV-------YAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSK 64

                          90       100
                  ....*....|....*....|....*..
gi 528501765 2148 NYHFMCARQQQCaFLEDKK--VYCQHH 2172
Cdd:cd15665    65 SFHFPCAAAAGC-FQDIKTltLFCPEH 90
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 4083-4218 7.24e-16

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: 80.28  E-value: 7.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKgigcYMFRIDDYE----VVDATIHGNSARFINHS 4158
Cdd:cd10541    96 LFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADKEGLEMGDE----YFANLDHIEescyIIDAKLEGNLGRYLNHS 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501765 4159 CEPNCYSRVVNVDGQKH----IVIFATRKIYKGEELTYDYKFPIEE-PGNKLPCNCGAKKCRKFL 4218
Cdd:cd10541   172 CSPNLFVQNVFVDTHDLrfpwVAFFASKRIKAGTELTWDYNYEVGSvEGKELLCCCGSNECRGRL 236
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 4090-4218 1.17e-15

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: 80.44  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4090 GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREK---YYDDKGIgcYMFRID---DYEVVDATIHGNS-----------A 4152
Cdd:cd19473   117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDaatIAQRKDV--YLFALDkfsDPDSLDPRLRGDPyeidgefmsgpT 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4153 RFINHSCEPN--CYSRVVNVdGQKHI---VIFATRKIYKGEELTYDY--------KFPIEEPGNKL--PCNCGAKKCRKF 4217
Cdd:cd19473   195 RFINHSCDPNlrIFARVGDH-ADKHIhdlAFFAIKDIPRGTELTFDYvdgvtgldDDAGDEEKEKEmtKCLCGSPKCRGY 273


                  .
gi 528501765 4218 L 4218
Cdd:cd19473   274 L 274
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2219-2266 6.88e-15

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: 71.38  E-value: 6.88e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528501765  2219 GSMTIDCLGMLTELS---DCERKLFPVGYQCSRVYWSTLDARKRCVYKCRI 2266
Cdd:pfam05964    1 GSLTVLSLGEIVPDRpafHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 2068-2172 1.19e-14

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: 72.60  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKtnDCGRL---LYIGHneWAHVNCALWSAEVYEdVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTS 2144
Cdd:cd15700     1 CCLCRNPANYK--DLGDLcgpYYPEH--WVHEACAVWTTGVYL-VAGKLFGLQEAVQKAADAKCSSCQGAGATVGCCHKG 75

                          90       100
                  ....*....|....*....|....*....
gi 528501765 2145 CTNNYHFMCARQQQCAFLEDK-KVYCQHH 2172
Cdd:cd15700    76 CTQSYHYICAVEAGCLFEEENfSLRCPKH 104
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 4083-4218 8.03e-14

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: 74.87  E-value: 8.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLT---------DKREKYYDDKGIGCYMFRI-----DDYEVVDATIH 4148
Cdd:cd10523   112 VFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSRARSpteplppklELPSENEVEVVTSWLILSKkrklrENVCFLDASKE 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501765 4149 GNSARFINHSCEPNCYSRVVNVDGQKH----IVIFATRKIYKGEELTYDYKFPI-EEPGNKLPCNCGAKKCRKFL 4218
Cdd:cd10523   192 GNVGRFLNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYSYDAgTSPEQEIPCLCGVNKCQKKI 266
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 4092-4201 1.26e-13

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: 72.05  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4092 GLFCRKNIEPGEMVIEYSGNVIR--SVLTDKREKYYDDKGIGCYMFRIDDYE-VVDATIHGNSARFINHSCEPNC--YSR 4166
Cdd:cd19183    15 GLFADRPIPAGDPIQELLGEIGLqsEYIADPENQYQILGAPKPHVFFHPQSPlYIDTRRSGSVARFIRRSCRPNAelVTV 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 528501765 4167 VVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEP 4201
Cdd:cd19183    95 ASDSGSVLKFVLYASRDISPGEEITIGWDWDNPHP 129
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 2068-2172 1.56e-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: 69.93  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNygDEKTNdcgrLLYIGHNE--WAHVNCALWSAEVYE---------DVDGALKNVHMAVSRGKQLQCKNCHKPGA 2136
Cdd:cd15712     1 CAFCPK--GEEYS----IMYFAQEQniAAHQNCLLYSSGFVEseeynplnlDRRFDVESVLNEIKRGKRLKCNFCRKKGA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 528501765 2137 TVSCCMTSCTNNYHFMCARQQQCAFLEDK-----KVYCQHH 2172
Cdd:cd15712    75 TVGCEERACRRSYHYFCALCDDAAIETDEvrgiyRVFCQKH 115
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 4089-4194 3.05e-13

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: 68.94  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4089 HGRGLFCRKNIEPGEMVIEYSGNVirSVLTDKREKYYDDKGIGCYMFRIddyevvdatihgnsARFINHSCEPNCysrVV 4168
Cdd:cd20071     9 KGRGLVATRDIEPGELILVEKPLV--SVPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA---VV 69

                          90       100
                  ....*....|....*....|....*.
gi 528501765 4169 NVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd20071    70 VFDGNGTLRVRALRDIKAGEELTISY 95
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
 2225-2267 8.12e-13

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: 65.38  E-value: 8.12e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 528501765   2225 CLGMLTELSDCERKLFPVGYQCSRVYWSTLDARKRCVYKCRIL 2267
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVID 43
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 2068-2172 6.48e-12

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: 64.98  E-value: 6.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNygdEKTNDCGRLLYI-GHNEWAHVNCALWSAEVY------EDVDG-ALKNVHMAVSRGKQLQCKNCHKPGATVS 2139
Cdd:cd15710     1 CGFCRS---NREKECGQLLISeNQKVAAHHKCMLFSSALVsshsdsENLGGfSIEDVQKEIKRGTKLMCSLCHCPGATIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 528501765 2140 CCMTSCTNNYHFMCARQQQCAFLEDKK-----VYCQHH 2172
Cdd:cd15710    78 CDVKTCHRTYHYYCALHDKAQIRENPSqgiymIYCRKH 115
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 4083-4194 1.31e-11

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: 67.43  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKyyDDKgigcYMFRID------------------------ 4138
Cdd:cd10545    90 VFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSG--NDD----YLFDIDnrqtnrgwdggqrldvgmsdgers 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 4139 DYE-------VVDATIHGNSARFINHSCEPNCYSRVVNVDGQK----HIVIFATRKIYKGEELTYDY 4194
Cdd:cd10545   164 SAEdeessefTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDlrlpRVMLFAADNIPPLQELTYDY 230
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
 2068-2172 1.88e-11

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: 63.40  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDEKtnDCGRLLYIGHNEWAHVNCALWSAEVYEdVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15699     1 CCLCGKWANYR--NLGDLFGPFYEFWVHEGCILWANGIYL-VCGRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSF 77

                          90       100
                  ....*....|....*....|....*.
gi 528501765 2148 NYHFMCARQQQCAFLEDK-KVYCQHH 2172
Cdd:cd15699    78 RYHYPCAIDADCLLNEENfSVRCPKH 103
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 2068-2172 5.30e-11

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: 62.79  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALClNYGDEKTNDCGRL-LYIGHNEWAHVNCALWSAEVY--------EDVDGALKNVHMAVSRGKQLQCKNCHKPGATV 2138
Cdd:cd15711     1 CGFC-HAGEEENETRGKLhIFNAKKAAAHYKCMLFSSGTVqltttsraEFGDFDIKTVIQEIKRGKRMKCTLCSQLGATI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 528501765 2139 SCCMTSCTNNYHFMCARQQQCAFLEDK-----KVYCQHH 2172
Cdd:cd15711    80 GCEIKACVKTYHYHCGVQDKAKYIENMsrgiyKLYCKNH 118
PHD6_KMT2C_like cd15514
PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in ...
 1763-1818 6.01e-11

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: 59.99  E-value: 6.01e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1763 CPLCNKGYDDDDcdsKMMKCKKCDRWVHAKCESL-TDDMCELMSslpeNVVYTCTNC 1818
Cdd:cd15514     2 CPVCSRSYNEGE---LIIQCSQCERWLHGACDSLrTEEEAERAA----DNGYRCLLC 51
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 2068-2154 6.80e-11

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: 61.47  E-value: 6.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALClnygdektnDCGRLlyighneWAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTN 2147
Cdd:cd15695     1 CALC---------NCGEC-------WVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPR 64


                  ....*..
gi 528501765 2148 NYHFMCA 2154
Cdd:cd15695    65 FYHFPCA 71
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 2093-2154 9.20e-11

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: 61.11  E-value: 9.20e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528501765 2093 WAHVNCALWSAEVYEDVDGALKNVHMAVSRGKQLQCKNCHKPGATVSCCMTSCTNNYHFMCA 2154
Cdd:cd15696    10 WAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 71
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
2066-2172 9.41e-11

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 61.59  E-value: 9.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  2066 RQCALCLNYGD--EKTNDcgrllyighNEWAHVNCALWSAEVyedvdgALKNVH----MAVSRGKQ----LQCKNCHKP- 2134
Cdd:pfam13832    1 VRCCLCPLRGGalKQTSD---------GRWVHVLCAIFVPEV------RFGNVAtmepIDVSRIPPerwkLKCVFCKKRs 65

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528501765  2135 GATVSCCMTSCTNNYHFMCARQQQCAF-LED-----KKVYCQHH 2172
Cdd:pfam13832   66 GACIQCSKGRCTTAFHVTCAQAAGVYMePEDwpnvvVIAYCQKH 109
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 1675-1724 1.23e-10

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: 59.25  E-value: 1.23e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKKrvWVCTKC 1724
Cdd:cd15489     1 SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNGK--WICPVC 48
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 2068-2172 1.46e-10

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: 61.31  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDE-KTNDCGRllyighnEWAHVNCALWSAEV-------YEDVDgalKNVHMAVSRgKQLQCKNCH-KPGATV 2138
Cdd:cd15671     1 CVLCPKKGGAmKSTKSGT-------KWVHVSCALWIPEVsigcpekMEPIT---KISHIPMSR-WALVCVLCKeKTGACI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 528501765 2139 SCCMTSCTNNYHFMCARQ-----QQCAFLEDKKV----YCQHH 2172
Cdd:cd15671    70 QCSVKSCKTAFHVTCAFQhglemKTILEDEDDEVkfksYCPKH 112
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1675-1724 2.20e-10

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: 58.38  E-value: 2.20e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 528501765   1675 FCHVCGRKYqKTKQLLECDKCRNSYHPECLGPnhPTRPTKKKRVWVCTKC 1724
Cdd:smart00249    1 YCSVCGKPD-DGGELLQCDGCDRWYHQTCLGP--PLLEEEPDGKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1627-1676 1.04e-09

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: 56.73  E-value: 1.04e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528501765  1627 VCFLCASSGN-VEFVFCQVCCEPFHLFCLGEAERPHDEQWENWCCRRCRFC 1676
Cdd:pfam00628    1 YCAVCGKSDDgGELVQCDGCDDWFHLACLGPPLDPAEIPSGEWLCPECKPK 51
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1675-1727 1.18e-09

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: 56.35  E-value: 1.18e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 528501765  1675 FCHVCGRkYQKTKQLLECDKCRNSYHPECLGPNhPTRPTKKKRVWVCTKCVRC 1727
Cdd:pfam00628    1 YCAVCGK-SDDGGELVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKPK 51
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
 2068-2172 4.03e-09

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: 57.34  E-value: 4.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGD--EKTNDcgrllyighNEWAHVNCALWSAEVY-------EDVDGAlknVHMAVSRGKqLQCKNC-HKPGAT 2137
Cdd:cd15670     1 CVLCPNKGGafKQTDD---------GRWAHVVCALWIPEVSfantvflEPIDGI---QNIPKARWK-LTCYICkKRMGAC 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 2138 VSCCMTSCTNNYHFMCARQ--------------QQCAFLEDKKVYCQHH 2172
Cdd:cd15670    68 IQCHKKNCYTAFHVTCAQQaglymkiepvkdpgNGTSDSVRKEAYCDKH 116
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
 4097-4196 7.40e-09

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: 56.82  E-value: 7.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4097 KNIEPGEMVIEYSGNVIRsvltdkREKYyddKGIGCYMFR----------IDDYEV-VDATIHGNSARFINHSCEPNCYS 4165
Cdd:cd19182    25 KDLPPDTLIIEYRGKFML------REQF---EANGYFFKRpypfvlfyskFHGLEMcVDARTFGNEARFIRRSCTPNAEV 95

                          90       100       110
                  ....*....|....*....|....*....|.
gi 528501765 4166 RVVNVDGQKHIVIFATRKIYKGEELTYDYKF 4196
Cdd:cd19182    96 RHVIEDGTIHLYIYSIRSIPKGTEITIAFDF 126
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 4083-4214 9.38e-09

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: 57.33  E-value: 9.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4083 VYRSAIHGRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKgigcYMF-----RIDDYEV-VDATIHGNSARFIN 4156
Cdd:cd19181    11 VTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRP----YPFvlfysKFNGVEMcVDARTFGNDARFIR 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4157 HSCEPNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDYKFPIEEPGNKLPCNC--GAKKC 4214
Cdd:cd19181    87 RSCTPNAEVRHMIADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCAChkGNRNC 146
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 4089-4194 1.28e-08

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


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 56.52  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4089 HGRGLFCRKNIEPGEmVIEYSGNVIrSVLTDKREKYYDDkgigcymfRIDDYEVVDATIHGNS------ARFINHSCEPN 4162
Cdd:cd10524    18 YGAKIIATKPIKKGE-KIHELCGCI-AELSEEEEALLRP--------GGNDFSVMYSSRKKCSqlwlgpAAFINHDCRPN 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 528501765 4163 CysRVVNVdGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd10524    88 C--KFVPT-GKSTACVKVLRDIEPGEEITVYY 116
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
 1762-1818 4.27e-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: 52.48  E-value: 4.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 1762 LCPLCNKGYDDDDCDSK-MMKCKKCDRWVHAKCESLTDDMCElMSSLPENVVYTCTNC 1818
Cdd:cd15615     1 FCILCGQVYEENEGDEKeWVQCDSCSEWVHFECDGRTGLGAF-KYAKSDGLQYVCPRC 57
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1763-1818 6.74e-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: 51.44  E-value: 6.74e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 528501765   1763 CPLCNKGYDDDDcdskMMKCKKCDRWVHAKCESLTDDmcelmsSLPENVVYTCTNC 1818
Cdd:smart00249    2 CSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLL------EEEPDGKWYCPKC 47
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 1763-1818 8.28e-08

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: 51.16  E-value: 8.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528501765 1763 CPLCNKGYDDDDcdsKMMKCKKCDRWVHAKCESLTddmcelMSSLPENVVYTCTNC 1818
Cdd:cd15489     2 CIVCGKGGDLGG---ELLQCDGCGKWFHADCLGPP------LSSFVPNGKWICPVC 48
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1763-1821 9.19e-08

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 51.34  E-value: 9.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 528501765  1763 CPLCNKgyddDDCDSKMMKCKKCDRWVHAKCESLTDDMCELMSSlpenvVYTCTNCTES 1821
Cdd:pfam00628    2 CAVCGK----SDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPECKPK 51
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 4090-4194 1.93e-07

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: 52.26  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4090 GRGLFCRKNIEPGEmVIEYSGnVIrsVLTDkrEKYYDDKG--IGCYMFRIDDYEVVDATihGNSARFiNHSCEPNCysRV 4167
Cdd:cd10540    11 GRGVFATRPIKKGE-VIEEAP-VI--VLPK--EEYQHLCKtvLDHYVFSWGDGCLALAL--GYGSMF-NHSYTPNA--EY 79

                          90       100
                  ....*....|....*....|....*..
gi 528501765 4168 VNVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd10540    80 EIDFENQTIVFYALRDIEAGEELTINY 106
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1627-1673 3.36e-07

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 49.52  E-value: 3.36e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 528501765   1627 VCFLCASSGN-VEFVFCQVCCEPFHLFCLGEAERPHDEQwENWCCRRC 1673
Cdd:smart00249    1 YCSVCGKPDDgGELLQCDGCDRWYHQTCLGPPLLEEEPD-GKWYCPKC 47
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
 1675-1724 5.00e-07

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


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 48.82  E-value: 5.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRkyqkTKQLLECDKCRNSYHPECLGPNHPTRPTKKkrvWVCTKC 1724
Cdd:cd15532     1 FCRVCKD----GGELLCCDGCPSSYHLHCLNPPLAEIPDGD---WFCPRC 43
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
 2068-2172 8.53e-07

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Drosophila melanogaster RNO. RNO is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating the transcription of key EGFR/Ras pathway regulators in the Drosophila eye. RNO contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.


Pssm-ID: 277177 [Multi-domain]  Cd Length: 113  Bit Score: 50.29  E-value: 8.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDE-KTNDCGrllyighNEWAHVNCALWSAEV----YEDVDGALKNVHMAVSRGkQLQCKNC-HKPGATVSCC 2141
Cdd:cd15707     1 CILCPNKGGAmKSTRSG-------TKWAHVSCALWIPEVsigcVEKMEPITKISSIPASRW-ALICVLCrERTGACIQCS 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 528501765 2142 MTSCTNNYHFMCARQQQC---AFLEDK-------KVYCQHH 2172
Cdd:cd15707    73 VKTCKTAYHVTCGFQHGLemkTILDEEsedgvklRSYCQKH 113
ePHD_BRPF1 cd15701
Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...
 2068-2156 1.18e-06

Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF1. BRPF1, also termed peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a 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 methylated lysine 4 of histone H3 (H3K4me), 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. BRPF1 may be involved in chromatin remodeling.


Pssm-ID: 277171 [Multi-domain]  Cd Length: 121  Bit Score: 50.46  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGDE-KTNDCGRllyighneWAHVNCALWSAEV-------YEDVDGAlknVHMAVSRGKqLQCKNCHK--PGAT 2137
Cdd:cd15701     1 CALCPNKGGAfKQTDDGR--------WAHVVCALWIPEVcfantvfLEPIDSI---EHIPPARWK-LTCYICKQrgSGAC 68

                          90
                  ....*....|....*....
gi 528501765 2138 VSCCMTSCTNNYHFMCARQ 2156
Cdd:cd15701    69 IQCHKANCYTAFHVTCAQQ 87
BROMO smart00297
bromo domain;
1899-1959 1.29e-06

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 49.58  E-value: 1.29e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501765   1899 PLDLESVEKKMDSGCYKSVLEFSDDIVKIIQTAFNSDGGQLESRKANSMLKSFFIRQMERI 1959
Cdd:smart00297   47 PMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
PHD5_KMT2D cd15601
PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
 1763-1818 1.32e-06

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (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 asHOXA1-3 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 downregulated in cholestasis. KMT2D contains the catalytic domain SET, five 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 fifth PHD finger.


Pssm-ID: 277074  Cd Length: 51  Bit Score: 47.98  E-value: 1.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1763 CPLCNKGYDDDDCdskMMKCKKCDRWVHAKCESL-TDDMCELMSslpeNVVYTCTNC 1818
Cdd:cd15601     2 CPVCRAKYVEEDL---LIQCRHCDRWVHAVCESLfTEDEVEQAA----DEGFDCSSC 51
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
 4149-4194 1.33e-06

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


Pssm-ID: 380937  Cd Length: 138  Bit Score: 50.49  E-value: 1.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 4149 GNSARFI----NHSCE----PNCYSRVVNVDGQKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd10539    72 GNIARFIsginNHTKDgkkkQNCKCVRYSINGEARVLLVATRDIAKGERLYYDY 125
PHD_UHRF1_2 cd15525
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...
 1676-1724 2.04e-06

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and UHRF2; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumour suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger.


Pssm-ID: 277000  Cd Length: 47  Bit Score: 47.36  E-value: 2.04e-06
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gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPTKKKrvWVCTKC 1724
Cdd:cd15525     2 CHVCGGKQDPEKQLL-CDECDMAYHLYCLDPPLTSLPDDDE--WYCPDC 47
ePHD_JADE3 cd15706
Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...
 2068-2154 2.37e-06

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: 49.34  E-value: 2.37e-06
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gi 528501765 2068 CALCLNYGDE-KTNDCGrllyighNEWAHVNCALWSAEVY----EDVDGALKNVHMAVSRGkQLQCKNCH-KPGATVSCC 2141
Cdd:cd15706     1 CLLCPKTGGAmKATRTG-------TKWAHVSCALWIPEVSiacpERMEPITKVSHIPPSRW-ALVCSLCKlKTGACIQCS 72

                          90
                  ....*....|...
gi 528501765 2142 MTSCTNNYHFMCA 2154
Cdd:cd15706    73 VKSCITAFHVTCA 85
PHD_UHRF1 cd15616
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); ...
 1676-1724 3.49e-06

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); UHRF1 (also termed inverted CCAAT box-binding protein of 90 kDa, nuclear protein 95, nuclear zinc finger protein Np95 (Np95), RING finger protein 106, transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1) is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumour suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET and RING finger associated (SRA) domain, and a C-terminal RING-finger domain. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitylation has an essential role in maintaining DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD finger targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-finger domain exhibit both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1.


Pssm-ID: 277088  Cd Length: 47  Bit Score: 46.50  E-value: 3.49e-06
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gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPTKKKrvWVCTKC 1724
Cdd:cd15616     2 CHVCGGKQDPDKQLM-CDECDMAFHIYCLNPPLSSIPDDED--WYCPEC 47
PHD3_KMT2C cd15511
PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
 1762-1818 4.73e-06

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: 46.33  E-value: 4.73e-06
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gi 528501765 1762 LCPLCNKGYDDDDCDSkMMKCKKCDRWVHAKCESLTDDmcELMSSLPENvvYTCTNC 1818
Cdd:cd15511     1 PCPACKKNLDPELQKD-MLHCHVCKRWIHLECEKPNDN--ELLDQLKED--YICSLC 52
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
 2092-2172 8.87e-06

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: 47.40  E-value: 8.87e-06
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gi 528501765 2092 EWAHVNCALWSAEVY----EDVDGALKNVHMAVSRGKqLQCKNCHK-PGATVSCCMTSCTNNYHFMCA----RQQQCAFL 2162
Cdd:cd15705    19 KWVHVSCALWIPEVSigcpEKMEPITKISHIPASRWA-LSCSLCKEcTGTCIQCSMPSCITAFHVTCAfdhgLEMRTTLA 97

                          90
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gi 528501765 2163 EDKKV----YCQHH 2172
Cdd:cd15705    98 DNDEVkfksFCLEH 111
PHD6_KMT2C cd15600
PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
 1763-1818 9.57e-06

PHD finger 6 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 sixth PHD finger.


Pssm-ID: 277073  Cd Length: 51  Bit Score: 45.31  E-value: 9.57e-06
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gi 528501765 1763 CPLCNKGYDDDDCdskMMKCKKCDRWVHAKCESL-TDDMCELMSslpeNVVYTCTNC 1818
Cdd:cd15600     2 CPICYRNYREEEL---ILQCRQCDRWMHASCQNLnTEEEVENAA----DNGFDCTMC 51
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 4130-4194 9.71e-06

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


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 49.60  E-value: 9.71e-06
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gi 528501765 4130 IGCYMFRIDDYEVVDAT--IHGNSARFI-----------NHSCEPNCysrVVNVDGQKhIVIFATRKIYKGEELTYDY 4194
Cdd:cd10536   116 LQCNAHAITELQTTSSGsqVDTSKQVRIataiyptlsllNHSCDPNT---IRSFYGNT-IVVRATRPIKKGEEITICY 189
ePHD_ATX1_2_like cd15662
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...
 2068-2155 1.12e-05

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: 1.12e-05
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gi 528501765 2068 CALC-LNYGDEKTNDCGRllyighneWAHVNCALWSAE--VYEDVDGALKNVHMAVSRGK-QLQCKNCHKP-GATVSCCM 2142
Cdd:cd15662     1 CCLCpVVGGALKPTTDGR--------WAHLACAIWIPEtcLLDVKTMEPVDGINAISKERwELSCTICKQRyGACIQCSN 72

                          90
                  ....*....|...
gi 528501765 2143 TSCTNNYHFMCAR 2155
Cdd:cd15662    73 NSCRVAYHPLCAR 85
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
 1676-1724 1.75e-05

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


Pssm-ID: 277002  Cd Length: 46  Bit Score: 44.68  E-value: 1.75e-05
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gi 528501765 1676 CHVCGRKyQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKkrvWVCTKC 1724
Cdd:cd15527     2 CSVCQDS-GNADNLLFCDACDKGFHMECHDPPLTRMPKGK---WVCQIC 46
PHD_UHRF2 cd15617
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...
 1676-1724 1.88e-05

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); UHRF2 (also termed Np95/ICBP90-like RING finger protein (NIRF), Np95-like RING finger protein, nuclear protein 97, nuclear zinc finger protein Np97, RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2) was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs,p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger.


Pssm-ID: 277089  Cd Length: 47  Bit Score: 44.56  E-value: 1.88e-05
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gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPnhPTRPTKKKRVWVCTKC 1724
Cdd:cd15617     2 CYVCGGKQDAHMQLL-CDECNMAYHIYCLNP--PLDKIPEDEDWYCPSC 47
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
 2068-2172 2.89e-05

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: 46.20  E-value: 2.89e-05
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gi 528501765 2068 CALCLNYGD--EKTNDcgrllyiGHneWAHVNCALWSAEV-------YEDVDGaLKNVHMAvsRGKqLQCKNCHKP--GA 2136
Cdd:cd15703     1 CVLCPNKGGafKQTSD-------GR--WAHVVCAIWIPEVcfantvfLEPVEG-VNNIPPA--RWK-LTCYLCKQKgrGA 67

                          90       100       110       120       130
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gi 528501765 2137 TVSCCMTSCTNNYHFMCARQ---------------QQCAFLEDKKVYCQHH 2172
Cdd:cd15703    68 AIQCHKVNCYTAFHVTCAQRaglfmkiepvretglNGTTFTVRKTAYCENH 118
PHD1_KDM5C_5D cd15604
PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...
 1676-1724 6.15e-05

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C (also termed Histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, SmcX, or Xe169) is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D (also termed Histocompatibility Y antigen (H-Y), Histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or SmcY) is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 andH3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. Both KDM5C and KDM5D contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.


Pssm-ID: 277077  Cd Length: 46  Bit Score: 42.91  E-value: 6.15e-05
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gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPtkkKRVWVCTKC 1724
Cdd:cd15604     2 CRMCSRGDEDDKLLL-CDGCDDNYHTFCLLPPLPEPP---KGIWRCPKC 46
PHD_Int12 cd15501
PHD finger found in integrator complex subunit 12 (Int12) and similar proteins; Int12, also ...
 1676-1724 6.32e-05

PHD finger found in integrator complex subunit 12 (Int12) and similar proteins; Int12, also termed IntS12, or PHD finger protein 22, is a component of integrator, a multi-protein mediator of small nuclear RNA processing. The integrator complex directly interacts with the C-terminal domain of RNA polymerase II (RNAPII) largest subunit and mediates the 3' end processing of small nuclear RNAs (snRNAs) U1 and U2. Different from other components of integrator, Int12 contains a PHD finger, which is not required for snRNA 3' end cleavage. Instead, Int12 harbors a small microdomain at its N-terminus which is necessary and sufficient for Int12 function; this microdomain facilitates Int12 binding to Int1 and promotes snRNA 3' end formation.


Pssm-ID: 276976  Cd Length: 52  Bit Score: 43.10  E-value: 6.32e-05
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gi 528501765 1676 CHVCGRKYQKTK-QLLECDKCRNSYHPECLGPNHPTRPTKKKR-VWVCTKC 1724
Cdd:cd15501     2 CVVCKQMDVTSGnQLVECQECHNLYHQECHKPPVTDKDVNDPRlVWYCSRC 52
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
 1675-1724 1.00e-04

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: 42.27  E-value: 1.00e-04
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gi 528501765 1675 FCHVCGRKYQkTKQLLECDKCRNSYHPECLGPNHPTRPTKKkrvWVCTKC 1724
Cdd:cd15522     1 ICPICKKPDD-GSPMIGCDECDDWYHWECVGITDEPPEEDD---WFCPKC 46
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 1899-1951 1.34e-04

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 43.90  E-value: 1.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 528501765 1899 PLDLESVEKKMDSGCYKSVLEFSDDIVKIIQTA--FNSDGGQLeSRKANSMLKSF 1951
Cdd:cd04369    42 PMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAktYNGPGSPI-YKDAKKLEKLF 95
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 1675-1721 1.66e-04

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: 41.55  E-value: 1.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 1675 FCHVCGrkyqKTKQLLECDK--CRNSYHPECLGPNHPtrPTKKkrvWVC 1721
Cdd:cd15568     1 ECFRCG----DGGDLVLCDFkgCPKVYHLSCLGLEKP--PGGK---WIC 40
PHD1_Rco1 cd15535
PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...
 1675-1724 1.77e-04

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


Pssm-ID: 277010 [Multi-domain]  Cd Length: 45  Bit Score: 41.64  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501765 1675 FCHVCGRkyqkTKQLLECDKCRNSYHPECLGPnhPTRPTKK-KRVWVCTKC 1724
Cdd:cd15535     1 FCSACGG----YGSFLCCDGCPRSFHFSCLDP--PLEEDNLpDDEWFCNEC 45
PHD1_KDM5A cd15602
PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...
 1676-1725 1.83e-04

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2)) was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.


Pssm-ID: 277075  Cd Length: 49  Bit Score: 41.86  E-value: 1.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPtkkKRVWVCTKCV 1725
Cdd:cd15602     2 CLFCGRGNNEDKLLL-CDGCDDSYHTFCLIPPLPDVP---KGDWRCPKCV 47
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
 2068-2156 1.94e-04

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: 43.88  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLNYGD--EKTNDcgrllyighNEWAHVNCALWSAEV-------YEDVDGaLKNVHMAvsRGKqLQCKNCHKP--GA 2136
Cdd:cd15702     1 CVLCPNKGGafKKTDD---------DRWGHVVCALWIPEVgfantvfIEPIDG-VRNIPPA--RWK-LTCYLCKQKgvGA 67

                          90       100
                  ....*....|....*....|
gi 528501765 2137 TVSCCMTSCTNNYHFMCARQ 2156
Cdd:cd15702    68 CIQCHKANCYTAFHVTCAQK 87
PHD_PHF21A cd15523
PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...
 1675-1724 2.07e-04

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


Pssm-ID: 276998 [Multi-domain]  Cd Length: 43  Bit Score: 41.61  E-value: 2.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCgrkyQKTKQLLECDKCRNSYHPECLGPNHPTRPtkkKRVWVCTKC 1724
Cdd:cd15523     1 FCSVC----RKSGELLMCDTCSLVYHLDCLDPPLKTIP---KGMWICPKC 43
PHD1_Lid_like cd15605
PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...
 1676-1724 2.27e-04

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar proteins; Drosophila melanogaster Lid, also termed Retinoblastoma-binding protein 2 homolog, is identified genetically as a trithorax group (trxG) protein that is a Drosophila homolog of the human protein JARID1A/kdm5A, a member of the JARID subfamily within the JmjC proteins. Lid functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Lid contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger of Lid.


Pssm-ID: 277078  Cd Length: 46  Bit Score: 41.28  E-value: 2.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPtkkKRVWVCTKC 1724
Cdd:cd15605     2 CHTCGRGDGEESMLL-CDGCDDSYHTFCLLPPLSEVP---KGDWRCPKC 46
PHD1_KDM5A_like cd15515
PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...
 1676-1724 2.27e-04

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar proteins; The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me2 and H3K4me3), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. This family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent H3K4me3 demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.


Pssm-ID: 276990  Cd Length: 46  Bit Score: 41.61  E-value: 2.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPTKKkrvWVCTKC 1724
Cdd:cd15515     2 CQVCGRGDDEDKLLL-CDGCDDSYHTFCLIPPLPDIPPGD---WRCPKC 46
PHD_PHRF1 cd15536
PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also ...
 1675-1724 2.40e-04

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


Pssm-ID: 277011  Cd Length: 46  Bit Score: 41.25  E-value: 2.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPTKKkrvWVCTKC 1724
Cdd:cd15536     1 YCEVCGRSDREDRLLL-CDGCDAGYHMECLTPPLDEVPIEE---WFCPEC 46
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
2066-2168 2.54e-04

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 47.28  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2066 RQCALCLNY-GDEKTNDCGRllyighneWAHVNCALWSAEVY-------EDVDGaLKNVhmAVSRGKqLQCKNCHKPGAT 2137
Cdd:COG5141   248 RCCSFCPSSdGAFKQTSDGR--------WGHVICAMFNPELSfghllskDPIDN-IASV--SSSRWK-LGCLICKEFGGT 315

                          90       100       110
                  ....*....|....*....|....*....|..
gi 528501765 2138 -VSCCMTSCTNNYHFMCARqQQCAFleDKKVY 2168
Cdd:COG5141   316 cIQCSYFNCTRAYHVTCAR-RAGYF--DLNIY 344
PHD2_PHF14 cd15562
PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
 1675-1724 3.12e-04

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the second PHD finger.


Pssm-ID: 277037  Cd Length: 50  Bit Score: 41.24  E-value: 3.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528501765 1675 FCHVCGrKYQKTKQLLECDKCRNSYHPECLGPnhP-TRPTKKKR--VWVCTKC 1724
Cdd:cd15562     1 SCGICK-KSNDQHLLALCDTCKLYYHLGCLDP--PlTRMPKKTKnsGWQCSEC 50
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
 1765-1818 3.14e-04

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: 41.23  E-value: 3.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 1765 LCNKGYDDDdcdsKMMKCKKCDRWVHAKCESLTDDMCELMSSLPENvvYTCTNC 1818
Cdd:cd15552     3 ICRKPHNNR----FMICCDRCEEWFHGDCVGITEAQGKEMEENIEE--YVCPKC 50
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
 1763-1799 3.25e-04

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: 41.12  E-value: 3.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 528501765 1763 CPLCNKGYDDddcdSKMMKCKKCDRWVHAKCESLTDD 1799
Cdd:cd15522     2 CPICKKPDDG----SPMIGCDECDDWYHWECVGITDE 34
PHD_BAZ2A_like cd15545
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...
 1675-1724 3.53e-04

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


Pssm-ID: 277020 [Multi-domain]  Cd Length: 46  Bit Score: 40.76  E-value: 3.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 1675 FCHVCgRKYQKTKQLLECDKCRNSYHPECLGPnhptrptKKKRV----WVCTKC 1724
Cdd:cd15545     1 SCQIC-RSGDNEDQLLLCDGCDRGYHTYCFKP-------KMTNVpegdWFCPEC 46
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 4130-4194 3.68e-04

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; 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. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.


Pssm-ID: 380980 [Multi-domain]  Cd Length: 210  Bit Score: 45.05  E-value: 3.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 4130 IGCYMFRIDDYEVVDATIhG--NSARFINHSCEPNCysrVVNVDGqKHIVIFATRKIYKGEELTYDY 4194
Cdd:cd19203   120 VTCNSFTICDAEMQEVGV-GlyPSASLLNHSCDPNC---VIVFNG-PHLLLRAIREIEVGEELTISY 181
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 1627-1673 5.26e-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: 40.38  E-value: 5.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 1627 VCFLCASSGNV--EFVFCQVCCEPFHLFCLGEAERPHDEQwENWCCRRC 1673
Cdd:cd15489     1 SCIVCGKGGDLggELLQCDGCGKWFHADCLGPPLSSFVPN-GKWICPVC 48
PHD4_NSD3 cd15658
PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
 1675-1724 7.41e-04

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


Pssm-ID: 277128  Cd Length: 40  Bit Score: 39.90  E-value: 7.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKyqktKQLLECDKCRNSYHPECLGPNHPtrptkkKRVWVCTKC 1724
Cdd:cd15658     1 FCFVCARG----GRLLCCESCPASFHPECLSIEMP------EGCWNCNEC 40
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 3221-3709 7.42e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 7.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3221 PLISETSERTMLALATEESEAGKSKKkTRTGSTVSSKSPQEGCADSQVPEGHMTPEHFIPPSVDGDHITSPGVAPVGETG 3300
Cdd:pfam03154   76 PLKSAKRQREKGASDTEEPERATAKK-SKTQEISRPNSPSEGEGESSDGRSVNDEGSSDPKDIDQDNRSTSPSIPSPQDN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3301 NQDMTRTSSTPVLPSSP-TLPLQNQKFIPATTVTSGPAPITSSAVQAAASQLKPGPEKLIvlnqhlqplyvlqTVPNGVM 3379
Cdd:pfam03154  155 ESDSDSSAQQQILQTQPpVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT-------------SQPPNQT 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3380 NPNAPVLTGLSGGISTSQSIFPAGSKGLVPVSHHPQihaftgTTQTGFQPVIPSTTSGLlIGVTSHDPQIGVTEAGHRHD 3459
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPP------PSQVSPQPLPQPSLHGQ-MPPMPHSLQTGPSHMQHPVP 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3460 HAP-NVAMVSSASTITPAPSMIPSGHGKKRLISRLQSPKSKKQARPKTQPtLAPSDvgpnMTLINLSPsqiaagiPAQTG 3538
Cdd:pfam03154  295 PQPfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP-LPPAP----LSMPHIKP-------PPTTP 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3539 LMELGTITATPHrkiPNIIKRPKQGVMylePTILPQP---MPISTTTQpgilGHDSSTHllPCTVSGLNTSQSvlnVVSV 3615
Cdd:pfam03154  363 IPQLPNPQSHKH---PPHLSGPSPFQM---NSNLPPPpalKPLSSLST----HHPPSAH--PPPLQLMPQSQQ---LPPP 427

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765  3616 PSSAPGNflgGSSVSLSAPGliSSTEITGSLSNLLIKA--NPHNLSLSEQPMVLHPGTP------MMSHLTNPAQTSIAS 3687
Cdd:pfam03154  428 PAQPPVL---TQSQSLPPPA--ASHPPTSGLHQVPSQSpfPQHPFVPGGPPPITPPSGPptstssAMPGIQPPSSASVSS 502

                          490       500
                   ....*....|....*....|....*....
gi 528501765  3688 SI-------CVFPPNQSITVPVNQQVEKE 3709
Cdd:pfam03154  503 SGpvpaavsCPLPPVQIKEEALDEAEEPE 531
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 2128-2172 1.03e-03

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 39.50  E-value: 1.03e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 528501765   2128 CKNCHKPGATVSCCMtsCTNNYHFMCARQQQCAFLEDKKVYCQHH 2172
Cdd:smart00249    5 CGKPDDGGELLQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 1628-1673 1.14e-03

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fourth PHD finger.


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 39.15  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1628 CFLCASSGNVefvfcqVCCE--P--FHLFCLGEaERPHDEQWEnwcCRRC 1673
Cdd:cd15567     2 CFICSEGGSL------ICCEscPasFHPECLGL-EPPPEGKFY---CEDC 41
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 4081-4194 1.33e-03

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: 41.90  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 4081 VGVYRSAIH--GRGLFCRKNIEPGEMVIEYSGNVIRSVLTDKREKYYDDKGIGcymfrIDDYEVVDATIHGNSARF---- 4154
Cdd:cd10530     9 VYVAESLIPsaGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTIS-----LDEETVIDVPEPYNSVSKycas 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 528501765 4155 ----INHSCEPNC-YSRVVN-VDGqkHI-VIFATRKIYKGEELTYDY 4194
Cdd:cd10530    84 lghkANHSFTPNCiYDPFVHpRFG--PIkCIRTLRAVEAGEELTVAY 128
PHD5_KMT2C_like cd15513
PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...
 1676-1725 1.40e-03

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 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, 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 fifth PHD finger of KMT2C and the fourth PHD finger of KMT2D.


Pssm-ID: 276988  Cd Length: 47  Bit Score: 39.38  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1676 CHVCGRKYQKTKQLLeCDKCRNSYHPECLGPNHPTRPtkkKRVWVCTKCV 1725
Cdd:cd15513     2 CEGCGKASDESRLLL-CDDCDISYHTYCLDPPLQTVP---KGGWKCKWCV 47
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 1762-1818 1.47e-03

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: 39.07  E-value: 1.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1762 LCPLCNKGYDDDDCDskMMKCKKCDRWVHAKCESLTDDMCELMSslpenvVYTCTNC 1818
Cdd:cd15517     1 VCGICNLETAAVDEL--WVQCDGCDKWFHQFCLGLSNERYADED------KFKCPNC 49
PHD_PRKCBP1 cd15538
PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...
 1673-1724 1.60e-03

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), or Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor; the RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.


Pssm-ID: 277013  Cd Length: 41  Bit Score: 38.85  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528501765 1673 CRFCHVCGrkyqktkQLLECDKCRNSYHPECLGPNhpTRPTKKkrvWVCTKC 1724
Cdd:cd15538     2 CWRCHKEG-------QVLCCSLCPRVYHKKCLKLT--SEPDED---WVCPEC 41
PHD_PHF21B cd15524
PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) ...
 1675-1724 1.72e-03

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


Pssm-ID: 276999 [Multi-domain]  Cd Length: 43  Bit Score: 38.72  E-value: 1.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKyqktKQLLECDKCRNSYHPECLGPNHPTRPtkkKRVWVCTKC 1724
Cdd:cd15524     1 HCAACKRG----GNLQPCGTCPRAYHLDCLDPPLKTAP---KGVWVCPKC 43
PHD3_PHF14 cd15563
PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
 1676-1724 1.80e-03

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the third PHD finger.


Pssm-ID: 277038  Cd Length: 49  Bit Score: 38.91  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501765 1676 CHVCGRKYQKTkQLLECDKCRNSYHPECLGPnhPTRPTKKKR--VWVCTKC 1724
Cdd:cd15563     2 CCVCKQTGDNS-QLVRCDECKLCYHFGCLDP--PLKKSPKQRgyGWVCEEC 49
PostSET smart00508
Cysteine-rich motif following a subset of SET domains;
4203-4219 2.15e-03

Cysteine-rich motif following a subset of SET domains;


Pssm-ID: 214703  Cd Length: 17  Bit Score: 38.16  E-value: 2.15e-03
                            10
                    ....*....|....*..
gi 528501765   4203 NKLPCNCGAKKCRKFLN 4219
Cdd:smart00508    1 KKQPCLCGAPNCRGFLG 17
PHD1_MTF2_PHF19_like cd15499
PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...
 1676-1725 2.17e-03

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins MTF2, PHF19, and similar proteins; The family includes two PCL family proteins, metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are homologs of PHD finger protein1 (PHF1). PCL family proteins are accessory components of the polycomb repressive complex 2 (PRC2) core complex and all contain an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. They specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD finger-containing proteins, the first PHD fingers of PCL proteins do not display histone H3K4 binding affinity and they do not affect the Tudor domain binding to histones. This model corresponds to the first PHD finger.


Pssm-ID: 276974  Cd Length: 53  Bit Score: 39.02  E-value: 2.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501765 1676 CHVCGRK-YQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKKRVWVCTKCV 1725
Cdd:cd15499     2 CSICGGAeARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGDEKWFCSRCV 52
PHD3_NSD cd15566
PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 1675-1723 2.55e-03

PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the third PHD finger.


Pssm-ID: 277041  Cd Length: 48  Bit Score: 38.56  E-value: 2.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528501765 1675 FCHVCGRKYQKTK-QLLECDKCRNSYHPECLGpnhPTRPTKKKRVWVCTK 1723
Cdd:cd15566     1 TCATCEASGDGSSgKLVRCIRCPRAYHAGCIP---AGSKLLNKKLIICPK 47
PHD_KDM2A_2B cd15555
PHD finger found in Lysine-specific demethylase KDM2A, KDM2B, and similar proteins; This ...
 1672-1724 2.55e-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: 38.92  E-value: 2.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528501765 1672 RCRFCHVCGRKYQKTKQLLECDKCRNSYHPECLGPNHPtRPTKKKRV---WVCTKC 1724
Cdd:cd15555     1 VCLICGEDGKEDEFETTLMECSICWEIVHPECLKEQGE-GGVVNEDLpnsWECPKC 55
Bromo_TBP7_like cd05491
Bromodomain; TBP7_like subfamily, limited to fungi. TBP7, or TAT-binding protein homolog 7, is ...
 1855-1948 3.09e-03

Bromodomain; TBP7_like subfamily, limited to fungi. TBP7, or TAT-binding protein homolog 7, is a yeast protein of unknown function that contains AAA-superfamily ATP-ase domains and a bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99923  Cd Length: 119  Bit Score: 40.51  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 1855 LRYRQAVMKPPELNPETE--ESLPSRRSPEGPDPPVLTEVSP-PNDSPLDLESVEKKMDSGCYKSVLEFSDDIVKIIQTA 1931
Cdd:cd05491    17 LKFEKPPTEDAFVRPDNEnnEERPYEIAKDKQGVDTILETASgKKFYNMDLDTIEERLWNGYYATPKDFLKDIKRIVRDA 96

                          90
                  ....*....|....*..
gi 528501765 1932 FNSdGGQLESRKANSML 1948
Cdd:cd05491    97 KTI-GDRERLLKANEMF 112
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
 1675-1724 3.17e-03

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


Pssm-ID: 277016 [Multi-domain]  Cd Length: 43  Bit Score: 38.09  E-value: 3.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501765 1675 FCHVCgrkyQKTKQLLECDKCRNSYHPEClgpnH-PTRPTKKKRVWVCTKC 1724
Cdd:cd15541     1 WCAVC----QNGGELLCCDKCPRVFHLDC----HiPPIPEFPSGEWSCSLC 43
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
 1766-1818 3.55e-03

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 38.07  E-value: 3.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528501765 1766 CNKGYDDDDcdSKMMKCKKCDRWVHAKCESLTDDMcelmssLPENvvYTCTNC 1818
Cdd:cd15550     2 CICGFEHDD--GFMICCDKCSVWQHGDCMGIDREN------IPDS--YLCEQC 44
PHD3_KMT2D cd15597
PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
 1676-1725 3.66e-03

PHD finger 3 found in Histone-lysine N-methyltransferase 2D (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 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 third PHD finger.


Pssm-ID: 277072  Cd Length: 51  Bit Score: 38.09  E-value: 3.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501765 1676 CHVCGRKYQKTK-QLLECDKCRNSYHPECLgpNHPTRPTKKKRVWVCTKCV 1725
Cdd:cd15597     3 CVVCGSFGRGSEgHLLACSQCSQCYHPYCV--NSKITKVMLLKGWRCVECI 51
ePHD_PHF14 cd15674
Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended ...
 2068-2164 4.26e-03

Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF14. PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and this non-canonical ePHD finger. It can interact with histones through its PHD fingers.


Pssm-ID: 277144  Cd Length: 114  Bit Score: 40.06  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501765 2068 CALCLN-YGDEKTNDCGRllyighneWAHVNCALWSAEV-YEDVDgALKNV---HMAVSRGKQLQCKNCHKP-----GAT 2137
Cdd:cd15674     1 CELCPNrGGIFKETDTGR--------WVHLVCALYTPGVaFGDVD-KLSPVtltEMNYSKWGARECSLCEDPrfartGVC 71

                          90       100
                  ....*....|....*....|....*..
gi 528501765 2138 VSCCMTSCTNNYHFMCArqQQCAFLED 2164
Cdd:cd15674    72 ISCDAGMCKSYFHVTCA--QREGLLSE 96
PHD1_PHF1 cd15500
PHD finger 1 found in PHD finger protein1 (PHF1); PHF1, also termed polycomb-like protein 1 ...
 1688-1724 4.69e-03

PHD finger 1 found in PHD finger protein1 (PHF1); PHF1, also termed polycomb-like protein 1 (PCL1), together with JARID2 and AEBP2, associates with the polycomb repressive complex 2 (PRC2), which is the major H3K27 methyltransferase that regulates pluripotency, differentiation, and tumorigenesis through catalysis of histone H3 lysine 27 trimethylation (H3K27me3) on chromatin. PHF1 is essential in epigenetic regulation and genome maintenance. It acts as a dual reader of Lysine trimethylation at Lysine 36 of Histone H3 and Lysine 27 of Histone variant H3t. PHF1 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. Its Tudor domain selectively binds to histone H3K36me3. Moreover, PHF1 is required for efficient H3K27me3 and Hox gene silencing. It can mediate deposition of the repressive H3K27me3 mark and acts as a cofactor in early DNA-damage response. This model corresponds to the first PHD finger.


Pssm-ID: 276975  Cd Length: 51  Bit Score: 37.89  E-value: 4.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 528501765 1688 QLLECDKCRNSYHPECLGPNHPTRPTKKKRVWVCTKC 1724
Cdd:cd15500    15 PLVNCEKCHHAYHQECHVPRVPLESAGDGDSWMCRQC 51
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
 2093-2154 4.98e-03

Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, 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 ATX3 (also termed protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also termed protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also termed protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. These proteins show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain proteins that consist of an N-terminal PWWP domain, a canonical PHD finger, this non-canonical extended PHD finger, and a C-terminal SET domain.


Pssm-ID: 277133  Cd Length: 112  Bit Score: 39.81  E-value: 4.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 2093 WAHVNCALWSAEV-YEDVDG-----ALKNVHMAVSRGKQLQCKNCHkpGATVSCCmtSCTNNYHFMCA 2154
Cdd:cd15663    20 WVHVTCAWFRPEVcFKNEEKmepavGLLRIPLSTFLKACVICKQIH--GSCTQCC--KCATYFHAMCA 83
PHD1_NSD3 cd15649
PHD finger 1 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
 1627-1674 5.16e-03

PHD finger 1 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the first PHD finger.


Pssm-ID: 277119  Cd Length: 44  Bit Score: 37.44  E-value: 5.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 1627 VCFLCASSGNvEFVFCQ-VCCEPFHLFCLGEAERPHDEqwenWCCRRCR 1674
Cdd:cd15649     1 VCQVCESFGE-SLVTCEgECCGLFHLECLGLTSLPDEK----FICQECK 44
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
 1675-1724 6.32e-03

PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers.


Pssm-ID: 277035  Cd Length: 47  Bit Score: 37.33  E-value: 6.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528501765 1675 FChVCGRKYQKTKQLLECDKCRNSYHPECLGpnhpTRPTKKKRV--WVCTKC 1724
Cdd:cd15560     1 YC-ICRTPYDESQFYIGCDRCQDWFHGRCVG----ILQSEAEKIdeYVCPQC 47
PHD1_Snt2p_like cd15497
PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...
 1670-1724 7.05e-03

PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the first canonical Cys4HisCys3 PHD finger.


Pssm-ID: 276972  Cd Length: 48  Bit Score: 37.29  E-value: 7.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501765 1670 CRRCR-FCHvcgrkyqkTKQLLECDKCRNSYHPECLGPnhP-TRPTKKKRVWVCTKC 1724
Cdd:cd15497     2 CKVCKeWCA--------SDDSVRCDECKVSYHLLCVDP--PlTKKPNRGFVWSCAPC 48
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
 2092-2154 7.41e-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: 39.28  E-value: 7.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528501765 2092 EWAHVNCALWSAEVY----EDVDGALKNVHMAVSRGKqLQCKNCH-KPGATVSCCMTSCTNNYHFMCA 2154
Cdd:cd15704    22 KWVHVSCALWIPEVSigspEKMEPITKVSHIPSSRWA-LVCSLCNeKVGASIQCSVKNCRTAFHVTCA 88
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 2128-2172 7.73e-03

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 37.30  E-value: 7.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 2128 CKNCHKPG----ATVSCCmtSCTNNYHFMCARQQQCAFLEDKKVYCQHH 2172
Cdd:cd15489     2 CIVCGKGGdlggELLQCD--GCGKWFHADCLGPPLSSFVPNGKWICPVC 48
PHD_RSF1 cd15543
PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...
 1676-1724 7.84e-03

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


Pssm-ID: 277018 [Multi-domain]  Cd Length: 46  Bit Score: 37.25  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528501765 1676 CHVCGRkYQKTKQLLECDKCRNSYHPECLGPNHPTRPTKKkrvWVCTKC 1724
Cdd:cd15543     2 CRKCGL-SDHPEWILLCDRCDAGYHTACLRPPLMIIPDGN---WFCPPC 46
PHD_Hop1p_like cd15558
PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and ...
 1766-1815 8.58e-03

PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and similar proteins; Fission yeast Hop1p, also termed linear element-associated protein hop1, is an S. pombe homolog of the synaptonemal complex (SC)-associated protein Hop1 in Saccharomyces cerevisiae. In contrast to S. cerevisiae, S. pombe forms thin threads, known as linear elements (LinEs), in meiotic nuclei, instead of a canonical synaptonemal complex. LinEs contain Rec10 protein and are evolutionary relics of SC axial elements. Fission yeast Hop1p is a linear element (LinE)-associated protein. It also associates with Rec10, which plays a role in recruiting the recombination machinery to chromatin. Hop1p contains an N-terminal HORMA (for Hop1p, Rev7p, and MAD2) domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277033  Cd Length: 47  Bit Score: 37.04  E-value: 8.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501765 1766 CNKGYDDddcdSKMMKCKKCDRWVHAKC---ESLTDdmcelmSSLPE-NVVYTC 1815
Cdd:cd15558     4 CGDWGED----GAMIQCAFCDTWQHLLCygfESAKD------PRIPDiHVCYRC 47
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
 1762-1798 8.94e-03

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


Pssm-ID: 277004  Cd Length: 44  Bit Score: 36.90  E-value: 8.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 528501765 1762 LCPLCNKGYDDDdcdsKMMKCKKCDRWVHAKCESLTD 1798
Cdd:cd15529     1 TCTKCGDPHDED----KMMFCDQCDRGYHTFCVGLRS 33
 
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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