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Conserved domains on  [gi|24639197|ref|NP_525040|]
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trithorax-related, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 2257-2409 5.25e-112

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: 352.12  E-value: 5.25e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2257 KSSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDA 2336
Cdd:cd19171    1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2337 TLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWM 2409
Cdd:cd19171   81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1877-1981 4.81e-56

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: 190.21  E-value: 4.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNS 1956
Cdd:cd15666    1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                         90       100
                 ....*....|....*....|....*
gi 24639197 1957 LYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15666   81 VYHLPCAIKDGCMFFKDKTMLCPSH 105
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 2105-2194 8.55e-33

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: 122.79  E-value: 8.55e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197    2105 EFRIQVQDagdkEPEREFRGSSPSAVWQQILQPITRLRKVHKWLQLFPQHISGEDLFGLTEPAIVRILESLPGIETLTDY 2184
Cdd:smart00542    1 LFRVEIES----DPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNY 76

                            90
                    ....*....|
gi 24639197    2185 RFKYGRNPLL 2194
Cdd:smart00542   77 WFRYHRSPLL 86
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2046-2097 4.46e-22

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: 91.03  E-value: 4.46e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24639197   2046 GNMTFLNVGQLLPHQLeAFHTPHYIYPIGYKVSRYYWCVRRPNRRCRYICSI 2097
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
PRK13914 super family cl36314
invasion associated endopeptidase;
602-830 1.17e-04

invasion associated endopeptidase;


The actual alignment was detected with superfamily member PRK13914:

Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 47.10  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   602 VLSKTTMAQQKPKMITTTTLSSQAA---LQMHHALIQDSSADKAGSSANSGSATSGASMQlKLTTANTPTKLSVSLAPDV 678
Cdd:PRK13914  143 VTSTPVAPTQEVKKETTTQQAAPAAetkTEVKQTTQATTPAPKVAETKETPVVDQNATTH-AVKSGDTIWALSVKYGVSV 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   679 VKLEEVGSESKAKLLVKQEAVVKDS--TGTPTSEER-----AEEIGTPEKRLNANATMTAinQVQNQSANQIQMATSTST 751
Cdd:PRK13914  222 QDIMSWNNLSSSSIYVGQKLAIKQTanTATPKAEVKteapaAEKQAAPVVKENTNTNTAT--TEKKETTTQQQTAPKAPT 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   752 ASNPSTPNPTV----NATPMNNQRSAAEDNALLKQLLQNNSSSHSLNQISITSAHVGSASASAPLSARKVINVRAPSMGK 827
Cdd:PRK13914  300 EAAKPAPAPSTntnaNKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGK 379


                  ...
gi 24639197   828 VRS 830
Cdd:PRK13914  380 AYS 382
PHA03255 super family cl31530
BDLF3; Provisional
 124-299 1.86e-03

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.20  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   124 SGTEMGAIKAEDADKQTFTSFTKKEGASSSASSSSSTASVISIEPSGSGQDHAENSGKSEDLDYVLMPASGADSSTSVGN 203
Cdd:PHA03255    4 ARDKAGAVLAMILICETSLIWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   204 STGTGTPAGTPIGATTSTIILN--ANNGTAGVSGAGTTTILTQKSghtnynifNTTATGSQTPTTTLLNRVNLHPKMktq 281
Cdd:PHA03255   84 TGTTVTPVPTTSNASTINVTTKvtAQNITATEAGTGTSTGVTSNV--------TTRSSSTTSATTRITNATTLAPTL--- 152

                         170
                  ....*....|....*...
gi 24639197   282 lmvNAKKLSEVTQTTAKV 299
Cdd:PHA03255  153 ---SSKGTSNATKTTAEL 167
 
Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 2257-2409 5.25e-112

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: 352.12  E-value: 5.25e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2257 KSSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDA 2336
Cdd:cd19171    1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2337 TLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWM 2409
Cdd:cd19171   81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1877-1981 4.81e-56

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: 190.21  E-value: 4.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNS 1956
Cdd:cd15666    1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                         90       100
                 ....*....|....*....|....*
gi 24639197 1957 LYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15666   81 VYHLPCAIKDGCMFFKDKTMLCPSH 105
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 2270-2392 1.25e-43

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: 155.19  E-value: 1.25e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197    2270 NNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNR-GIYMFRLDEDRVVDATLSGGLARYINH 2348
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 24639197    2349 SCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDE 2392
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
2271-2408 4.03e-41

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 148.57  E-value: 4.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2271 NVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRgiYMFRLDEDRVVDATLSGGLARYINHSC 2350
Cdd:COG2940    7 RIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSC 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24639197 2351 NPNCVTEIvevdRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHkiPCACgaPNCRKW 2408
Cdd:COG2940   85 DPNCEADE----EDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRC--PNCRGT 134
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 2105-2194 8.55e-33

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: 122.79  E-value: 8.55e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197    2105 EFRIQVQDagdkEPEREFRGSSPSAVWQQILQPITRLRKVHKWLQLFPQHISGEDLFGLTEPAIVRILESLPGIETLTDY 2184
Cdd:smart00542    1 LFRVEIES----DPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNY 76

                            90
                    ....*....|
gi 24639197    2185 RFKYGRNPLL 2194
Cdd:smart00542   77 WFRYHRSPLL 86
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 2281-2386 8.85e-31

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: 118.39  E-value: 8.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   2281 GLGLYAARDIEKHTMIIEYIGE-VIRTEVSEIREKQYESKNR----GIYMFRLDED--RVVDAT--LSGGLARYINHSCN 2351
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 24639197   2352 PNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYK 2386
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2103-2189 2.42e-30

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: 115.78  E-value: 2.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   2103 KPEFRIQVQDagdkEPEREFRGSSPSAVWQQILQPITRLRKVHKWLQLFPQHISGEDLFGLTEPAIVRILESLPGIETLT 2182
Cdd:pfam05965    1 GPLFRVTVEE----DPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCT 76


                   ....*..
gi 24639197   2183 DYRFKYG 2189
Cdd:pfam05965   77 NYKFRYG 83
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2046-2097 4.46e-22

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: 91.03  E-value: 4.46e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24639197   2046 GNMTFLNVGQLLPHQLeAFHTPHYIYPIGYKVSRYYWCVRRPNRRCRYICSI 2097
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
 2056-2099 1.43e-17

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: 78.09  E-value: 1.43e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24639197    2056 LLPHQLEAFHTPHYIYPIGYKVSRYYWCVRRPNRRCRYICSIAE 2099
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 1904-1981 2.83e-12

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: 64.66  E-value: 2.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   1904 HLNCALWSNGVY--ETVSGA--LMNFQTALQAGLSQACSACHQP-GATIKCFKSRCNSLYHLPCAIREECVF-YKNKSV- 1976
Cdd:pfam13771    1 HVVCALWSPELVqrGNDSMGfpIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDNGt 80


                   ....*...
gi 24639197   1977 ---HCSVH 1981
Cdd:pfam13771   81 fksYCKKH 88
PRK13914 PRK13914
invasion associated endopeptidase;
602-830 1.17e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 47.10  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   602 VLSKTTMAQQKPKMITTTTLSSQAA---LQMHHALIQDSSADKAGSSANSGSATSGASMQlKLTTANTPTKLSVSLAPDV 678
Cdd:PRK13914  143 VTSTPVAPTQEVKKETTTQQAAPAAetkTEVKQTTQATTPAPKVAETKETPVVDQNATTH-AVKSGDTIWALSVKYGVSV 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   679 VKLEEVGSESKAKLLVKQEAVVKDS--TGTPTSEER-----AEEIGTPEKRLNANATMTAinQVQNQSANQIQMATSTST 751
Cdd:PRK13914  222 QDIMSWNNLSSSSIYVGQKLAIKQTanTATPKAEVKteapaAEKQAAPVVKENTNTNTAT--TEKKETTTQQQTAPKAPT 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   752 ASNPSTPNPTV----NATPMNNQRSAAEDNALLKQLLQNNSSSHSLNQISITSAHVGSASASAPLSARKVINVRAPSMGK 827
Cdd:PRK13914  300 EAAKPAPAPSTntnaNKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGK 379


                  ...
gi 24639197   828 VRS 830
Cdd:PRK13914  380 AYS 382
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
1875-1977 9.50e-04

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 44.59  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1875 RQCVFCnqrgdgqadgPSRLLNF---DVDKWVHLNCALWSNGVY--ETVSGALMNFQTALQAGLSQA-CSACHQPGAT-I 1947
Cdd:COG5141  248 RCCSFC----------PSSDGAFkqtSDGRWGHVICAMFNPELSfgHLLSKDPIDNIASVSSSRWKLgCLICKEFGGTcI 317

                         90       100       110
                 ....*....|....*....|....*....|
gi 24639197 1948 KCFKSRCNSLYHLPCAiREECVFYKNKSVH 1977
Cdd:COG5141  318 QCSYFNCTRAYHVTCA-RRAGYFDLNIYSH 346
PHA03255 PHA03255
BDLF3; Provisional
 124-299 1.86e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.20  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   124 SGTEMGAIKAEDADKQTFTSFTKKEGASSSASSSSSTASVISIEPSGSGQDHAENSGKSEDLDYVLMPASGADSSTSVGN 203
Cdd:PHA03255    4 ARDKAGAVLAMILICETSLIWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   204 STGTGTPAGTPIGATTSTIILN--ANNGTAGVSGAGTTTILTQKSghtnynifNTTATGSQTPTTTLLNRVNLHPKMktq 281
Cdd:PHA03255   84 TGTTVTPVPTTSNASTINVTTKvtAQNITATEAGTGTSTGVTSNV--------TTRSSSTTSATTRITNATTLAPTL--- 152

                         170
                  ....*....|....*...
gi 24639197   282 lmvNAKKLSEVTQTTAKV 299
Cdd:PHA03255  153 ---SSKGTSNATKTTAEL 167
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1937-1981 2.42e-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: 37.96  E-value: 2.42e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 24639197    1937 CSACHQP---GATIKCfkSRCNSLYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:smart00249    2 CSVCGKPddgGELLQC--DGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
 
Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 2257-2409 5.25e-112

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: 352.12  E-value: 5.25e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2257 KSSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDA 2336
Cdd:cd19171    1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2337 TLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWM 2409
Cdd:cd19171   81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
 2256-2409 8.77e-81

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: 263.03  E-value: 8.77e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2256 SKSSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVD 2335
Cdd:cd19208    1 SKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVID 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24639197 2336 ATLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWM 2409
Cdd:cd19208   81 ATLTGGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 154
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 2258-2406 4.81e-77

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: 252.13  E-value: 4.81e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2258 SSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKN-RGIYMFRLDEDRVVDA 2336
Cdd:cd10518    2 SKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVIDA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2337 TLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEsHKIPCACGAPNCR 2406
Cdd:cd10518   82 TKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDE-EKIPCLCGAPNCR 150
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 2255-2409 1.09e-76

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: 251.15  E-value: 1.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2255 HSKSSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVV 2334
Cdd:cd19209    1 HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24639197 2335 DATLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWM 2409
Cdd:cd19209   81 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 2258-2410 7.12e-67

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: 223.04  E-value: 7.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2258 SSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDAT 2337
Cdd:cd19170    2 AMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDAT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2338 LSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEshKIPCACGAPNCRKWMN 2410
Cdd:cd19170   82 MHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDV--KIPCTCGSKKCRKYLN 152
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 2257-2406 5.09e-58

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: 197.56  E-value: 5.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2257 KSSQYKKMKQEWRnnvyLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESknRGI---YMFRLDEDRV 2333
Cdd:cd19169    4 KFNQLKFRKKQLK----FAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEA--IGIgssYLFRVDDDTI 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2334 VDATLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEshKIPCACGAPNCR 2406
Cdd:cd19169   78 IDATKCGNLARFINHSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDE--KIPCLCGAPQCR 148
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1877-1981 4.81e-56

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: 190.21  E-value: 4.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNS 1956
Cdd:cd15666    1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                         90       100
                 ....*....|....*....|....*
gi 24639197 1957 LYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15666   81 VYHLPCAIKDGCMFFKDKTMLCPSH 105
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 2269-2406 1.17e-54

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: 188.02  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2269 RNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRG-IYMFRLDEDRVVDATLSGGLARYIN 2347
Cdd:cd20072   12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDATKKGNIARFIN 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24639197 2348 HSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEshKIPCACGAPNCR 2406
Cdd:cd20072   92 HCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREED--KIPCLCGAPNCR 148
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 2260-2410 1.48e-54

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: 187.92  E-value: 1.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2260 QYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDATLS 2339
Cdd:cd19206    4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDATMH 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639197 2340 GGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWMN 2410
Cdd:cd19206   84 GNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 2260-2410 5.20e-47

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: 166.35  E-value: 5.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2260 QYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDATLS 2339
Cdd:cd19207    4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639197 2340 GGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWMN 2410
Cdd:cd19207   84 GNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 154
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 2270-2392 1.25e-43

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: 155.19  E-value: 1.25e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197    2270 NNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNR-GIYMFRLDEDRVVDATLSGGLARYINH 2348
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 24639197    2349 SCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDE 2392
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 2271-2409 8.49e-43

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: 153.51  E-value: 8.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2271 NVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYE-SKNRGIYMFRLDEDRVVDATLSGGLARYINHS 2349
Cdd:cd19172    3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYArEGNRHYYFMALKSDEIIDATKKGNLSRFINHS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2350 CNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKiPCACGAPNCRKWM 2409
Cdd:cd19172   83 CEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFERYGKEAQ-KCYCGSPNCRGYI 141
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
2271-2408 4.03e-41

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 148.57  E-value: 4.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2271 NVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRgiYMFRLDEDRVVDATLSGGLARYINHSC 2350
Cdd:COG2940    7 RIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSC 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24639197 2351 NPNCVTEIvevdRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHkiPCACgaPNCRKW 2408
Cdd:COG2940   85 DPNCEADE----EDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRC--PNCRGT 134
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 2269-2410 4.54e-41

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: 149.05  E-value: 4.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2269 RNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGI-YMFRLDEDRVVDATLSGGLARYIN 2347
Cdd:cd19205   13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDATKCGNFARFIN 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2348 HSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEshKIPCACGAPNCRKWMN 2410
Cdd:cd19205   93 HSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDV--KIPCLCGSENCRGTLN 153
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 1877-1981 7.65e-41

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: 146.74  E-value: 7.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNS 1956
Cdd:cd15698    1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                         90       100
                 ....*....|....*....|....*
gi 24639197 1957 LYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15698   81 VYHFACAIRAKCMFFKDKTMLCPMH 105
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 2271-2406 1.22e-40

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: 147.40  E-value: 1.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2271 NVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIR-TEVSEIREKQYESKNRGIYMFRLDEDRVVDATLSGGLARYINHS 2349
Cdd:cd10531    1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDkKEFKERLDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFINHS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24639197 2350 CNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEShKIPCACGAPNCR 2406
Cdd:cd10531   81 CEPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNYNEA-KQVCLCGAQNCR 136
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 2257-2410 4.69e-40

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: 146.32  E-value: 4.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2257 KSSQYKKMKQEWRnnvyLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGI-YMFRLDEDRVVD 2335
Cdd:cd19204    5 KLNQLKFRKKKLR----FGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIID 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24639197 2336 ATLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDesHKIPCACGAPNCRKWMN 2410
Cdd:cd19204   81 ATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIED--NKIPCLCGTENCRGTLN 153
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 1877-1981 6.59e-40

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: 144.03  E-value: 6.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNS 1956
Cdd:cd15697    1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                         90       100
                 ....*....|....*....|....*
gi 24639197 1957 LYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15697   81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 2281-2409 9.88e-37

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


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 136.01  E-value: 9.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2281 GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESK-NRGIYMFRLDEDRVVDATLSGGLARYINHSCNPNCVTEIV 2359
Cdd:cd19175   11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKgEKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 24639197 2360 EVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKipCACGAPNCRKWM 2409
Cdd:cd19175   91 QVDGETRIGVFAIRDIKKGEELTYDYQFVQFGADQD--CHCGSKNCRGKL 138
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 2272-2385 1.61e-35

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: 131.98  E-value: 1.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2272 VYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGiYMFRLDEDRVVDATLSGGLARYINHSCN 2351
Cdd:cd10519    3 LLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSN 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 24639197 2352 PNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd10519   82 PNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDY 115
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 2281-2405 7.52e-35

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: 130.90  E-value: 7.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2281 GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKN-RGIYMFRLDEDRVVDATLSGGLARYINHSCNPNCVTEIV 2359
Cdd:cd19173   13 GWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNiTNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQPNCETQKW 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 24639197 2360 EVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEShKIPCACGAPNC 2405
Cdd:cd19173   93 TVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNE-KKVCRCGAPNC 137
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 2276-2410 1.25e-33

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: 127.41  E-value: 1.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2276 RSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDATLSGGLARYINHSCNPNCV 2355
Cdd:cd19174    6 RTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSCDPNCE 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24639197 2356 TEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWMN 2410
Cdd:cd19174   86 MQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG 140
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
 2105-2194 8.55e-33

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: 122.79  E-value: 8.55e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197    2105 EFRIQVQDagdkEPEREFRGSSPSAVWQQILQPITRLRKVHKWLQLFPQHISGEDLFGLTEPAIVRILESLPGIETLTDY 2184
Cdd:smart00542    1 LFRVEIES----DPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNY 76

                            90
                    ....*....|
gi 24639197    2185 RFKYGRNPLL 2194
Cdd:smart00542   77 WFRYHRSPLL 86
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 1877-1981 4.55e-31

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: 118.66  E-value: 4.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNS 1956
Cdd:cd15664    1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                         90       100
                 ....*....|....*....|....*
gi 24639197 1957 LYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15664   81 NYHFMCARKAECVFQDDKKVFCPAH 105
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 2281-2386 8.85e-31

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: 118.39  E-value: 8.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   2281 GLGLYAARDIEKHTMIIEYIGE-VIRTEVSEIREKQYESKNR----GIYMFRLDED--RVVDAT--LSGGLARYINHSCN 2351
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 24639197   2352 PNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYK 2386
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2103-2189 2.42e-30

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: 115.78  E-value: 2.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   2103 KPEFRIQVQDagdkEPEREFRGSSPSAVWQQILQPITRLRKVHKWLQLFPQHISGEDLFGLTEPAIVRILESLPGIETLT 2182
Cdd:pfam05965    1 GPLFRVTVEE----DPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCT 76


                   ....*..
gi 24639197   2183 DYRFKYG 2189
Cdd:pfam05965   77 NYKFRYG 83
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 2281-2409 3.82e-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: 118.16  E-value: 3.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2281 GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRgIYMFRLDEDR-----VVDATLSGGLARYINHSCNPNCV 2355
Cdd:cd10542   99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDYNDddceyTVDAAYYGNISHFINHSCDPNLA 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24639197 2356 TEIVEVD-RDV---RIIIFAKRKIYRGEELSYDYKFDIEDESH----------KIPCACGAPNCRKWM 2409
Cdd:cd10542  178 VYAVWINhLDPrlpRIAFFAKRDIKAGEELTFDYLMTGTGGSSestipkpkdvRVPCLCGSKNCRKYL 245
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 1875-1981 6.43e-29

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: 112.79  E-value: 6.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1875 RQCVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRC 1954
Cdd:cd15693    1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                         90       100
                 ....*....|....*....|....*..
gi 24639197 1955 NSLYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15693   81 TSNYHFMCSRAKNCVFLEDKKVYCQRH 107
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 2274-2405 3.54e-28

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: 112.01  E-value: 3.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2274 LARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTE--VSEIREKQyESKNRGIYMFRLDEDRVVDATLSGGLARYINHSCN 2351
Cdd:cd19211    6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEecMARIKHAH-ENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQ 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24639197 2352 PNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDeSHKIPCACGAPNC 2405
Cdd:cd19211   85 PNCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLG-NEKTVCRCGAPNC 137
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 2280-2405 3.04e-26

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: 106.16  E-value: 3.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2280 QGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQ-YESKNRGIYMFRLDEDRVVDATLSGGLARYINHSCNPNCVTEI 2358
Cdd:cd19212   12 RGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRaHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQK 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 24639197 2359 VEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIpCACGAPNC 2405
Cdd:cd19212   92 WTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTE-CHCGADNC 137
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 2272-2405 9.34e-26

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


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 105.01  E-value: 9.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2272 VYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTE--VSEIREKQyESKNRGIYMFRLDEDRVVDATLSGGLARYINHS 2349
Cdd:cd19210    4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEecRARIRYAQ-EHDITNFYMLTLDKDRIIDAGPKGNYARFMNHC 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24639197 2350 CNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDEShKIPCACGAPNC 2405
Cdd:cd19210   83 CQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNG-KTVCKCGAPNC 137
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 2268-2387 1.71e-25

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: 103.45  E-value: 1.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2268 WRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYEsKNRGIYMFRLDEDRVVDATLSGGLARYIN 2347
Cdd:cd19218    2 SKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFAN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 24639197 2348 HSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKF 2387
Cdd:cd19218   81 HSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 2276-2409 3.76e-25

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: 107.00  E-value: 3.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2276 RSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQyESKNRGIYMFRLDE----DRV----VDATLSGGLARYIN 2347
Cdd:cd10544   96 KTPKKGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTKS-QTKGDMNYIIVLREhlssGKVletfVDPTYIGNIGRFLN 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24639197 2348 HSCNPNCVTEIVEVDRDV-RIIIFAKRKIYRGEELSYDY------------KFDIEDESHKIPCACGAPNCRKWM 2409
Cdd:cd10544  175 HSCEPNLFMVPVRVDSMVpKLALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSRKPCLCGAENCRGFL 249
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 2276-2385 1.92e-24

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: 103.60  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2276 RSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYeSKNRGIYMFRLDEDR---------VVDATLSGGLARYI 2346
Cdd:cd10538   95 RTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIY-DKSGGSYLFDLDEFSdsdgdgeelCVDATFCGNVSRFI 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24639197 2347 NHSCNPNCVTEIVEVDRD----VRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd10538  174 NHSCDPNLFPFNVVIDHDdlryPRIALFATRDILPGEELTFDY 216
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 2278-2385 3.59e-24

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: 100.34  E-value: 3.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2278 KIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYES-KNRGIYMF---RLDEDRVVDATL-SGGLARYINHSC-N 2351
Cdd:cd10528   25 DGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYAKdPSTGCYMYyfqYKGKTYCVDATKeSGRLGRLINHSKkK 104

                         90       100       110
                 ....*....|....*....|....*....|....
gi 24639197 2352 PNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd10528  105 PNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 2269-2391 2.16e-23

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


Pssm-ID: 380994  Cd Length: 136  Bit Score: 97.83  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2269 RNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYEsKNRGIYMFRLDEDRVVDATLSGGLARYINH 2348
Cdd:cd19217    5 KKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANH 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24639197 2349 SCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIED 2391
Cdd:cd19217   84 SVNPNCYAKVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQAD 126
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 1877-1981 9.45e-23

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: 95.34  E-value: 9.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPsRLLNFDVDKWVHLNCALWSNGVY--ETVSGALMNFQTALQAGLSQACSACHQP-GATIKCFKSR 1953
Cdd:cd15571    1 CALCPRSGGALKGGG-ALKTTSDGLWVHVVCALWSPEVYfdDGTLLEVEGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 24639197 1954 CNSLYHLPCAIREECVF-----YKNKSVHCSVH 1981
Cdd:cd15571   80 CPRSFHVSCAIRAGCLFefedgPGNFVVYCPKH 112
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 1877-1981 1.12e-22

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: 94.72  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNS 1956
Cdd:cd15694    1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                         90       100
                 ....*....|....*....|....*
gi 24639197 1957 LYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15694   81 NFHFMCARASRCCFQDDKKVFCQKH 105
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 2281-2385 2.45e-22

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: 94.33  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2281 GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNrgiYMFRLDED-RVVDATLSGGLARYINHSCNPNCVTEIV 2359
Cdd:cd10522   14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPL---YPFDLNGDiLVIDAGKKGNLTRFINHSDQPNLELIVR 90

                         90       100
                 ....*....|....*....|....*.
gi 24639197 2360 EVDRDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd10522   91 TLKGEQHIGFVAIRDIKPGEELFISY 116
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
 2046-2097 4.46e-22

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: 91.03  E-value: 4.46e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24639197   2046 GNMTFLNVGQLLPHQLeAFHTPHYIYPIGYKVSRYYWCVRRPNRRCRYICSI 2097
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 2280-2409 1.36e-20

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: 93.80  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2280 QGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYEsKNRGIYMFRLD--ED-RVVDATLSGGLARYINHSCNPNCVT 2356
Cdd:cd10525   97 RGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYD-RQGATYLFDLDyvEDvYTVDAAYYGNISHFVNHSCDPNLQV 175

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639197 2357 EIVEVD----RDVRIIIFAKRKIYRGEELSYDYKFDIED---ESHK-------------------IPCACGAPNCRKWM 2409
Cdd:cd10525  176 YNVFIDnldeRLPRIALFATRTIRAGEELTFDYNMQVDPvdaESTKmdsnfglaglpgspkkrvrIECKCGVRSCRKYL 254
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 2280-2409 2.19e-20

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: 92.65  E-value: 2.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2280 QGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKnrGI-YMFRLD---EDRVVDATLSGGLARYINHSCNPNCV 2355
Cdd:cd10532   95 RGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSK--GItYLFDLDyesDEFTVDAARYGNVSHFVNHSCDPNLQ 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639197 2356 TEIVEVD----RDVRIIIFAKRKIYRGEELSYDYKF----DIEDES---------HKIPCACGAPNCRKWM 2409
Cdd:cd10532  173 VFNVFIDnldtRLPRIALFSTRTIKAGEELTFDYQMkgsgDLSSDSidnspakkrVRTVCKCGAVTCRGYL 243
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 2276-2409 5.64e-20

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: 91.86  E-value: 5.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2276 RSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYEskNRGI-YMFRLD--EDRV-----VDATLSGGLARYIN 2347
Cdd:cd20073   99 KTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYD--NVGVtYLFDLDlfEDQVdeyytVDAQYCGDVTRFIN 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2348 HSCNPNCVTEIVEVDRDVRII----IFAKRKIYRGEELSYDYKFDIEDE----------------SHKIPCACGAPNCRK 2407
Cdd:cd20073  177 HSCDPNLAIYSVLRDKSDSKIydlaFFAIKDIPALEELTFDYSGRNNFDqlgfignrsnskyinlKNKRPCYCGSANCRG 256


                 ..
gi 24639197 2408 WM 2409
Cdd:cd20073  257 WL 258
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
 2272-2385 2.51e-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: 86.09  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2272 VYLARSKIQ-GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRgIYMFRLDEDRVVDATLSGGLARYINHSC 2350
Cdd:cd19168    3 VVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVSY-LYLFEEQEGIWVDAAIYGNLSRYINHAT 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 24639197 2351 NP----NCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd19168   82 DKvktgNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 1877-1981 4.96e-19

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: 84.28  E-value: 4.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFC----NQRGDGQADGPSrllnFDVdkWVHLNCALWSNGVYeTVSGALMNFQTALQAGLSQACSACHQPGATIKCFKS 1952
Cdd:cd15668    1 CVFCkrgpHYKGLGDLFGPY----YEV--WVHEDCAVWAPGVY-LVGGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHK 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 24639197 1953 RCNSLYHLPCAIREECVFYK-NKSVHCSVH 1981
Cdd:cd15668   74 GCKAKYHYPCAVESGCQLDEeNFSLLCPKH 103
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 2271-2385 1.58e-18

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: 81.53  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2271 NVYLARSKIQGLGLYAARDIEKhtmiieyiGEVIrtevseirekqyesknrgiymfrldedrvvdatlsgGLARYINHSC 2350
Cdd:cd08161    1 EIRPSTIPGAGFGLFATRDIPK--------GEVI------------------------------------GLARFINHSC 36

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 24639197 2351 NPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd08161   37 EPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 2269-2406 7.05e-18

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: 85.08  E-value: 7.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2269 RNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKqyESknrgiYMFRLD----EDRVVDATLSGGLAR 2344
Cdd:cd10543   90 RYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRED--DS-----YLFDLDnkdgETYCIDARRYGNISR 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639197 2345 YINHSCNPNCVTEIVEVD-RDVR---IIIFAKRKIYRGEELSYDY--KF-DIedESHKIPCACGAPNCR 2406
Cdd:cd10543  163 FINHLCEPNLIPVRVFVEhQDLRfprIAFFASRDIKAGEELGFDYgeKFwRI--KGKYFTCRCGSPKCK 229
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 2281-2409 9.91e-18

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


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 85.83  E-value: 9.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2281 GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNR-GIYMFRLD---EDRVVDATLSG-----------GLARY 2345
Cdd:cd19473  117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAATIAQRkDVYLFALDkfsDPDSLDPRLRGdpyeidgefmsGPTRF 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2346 INHSCNPNcvTEIVEVDRDV------RIIIFAKRKIYRGEELSYDY----------KFDIEDESHKIPCACGAPNCRKWM 2409
Cdd:cd19473  197 INHSCDPN--LRIFARVGDHadkhihDLAFFAIKDIPRGTELTFDYvdgvtgldddAGDEEKEKEMTKCLCGSPKCRGYL 274
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
 2056-2099 1.43e-17

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: 78.09  E-value: 1.43e-17
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24639197    2056 LLPHQLEAFHTPHYIYPIGYKVSRYYWCVRRPNRRCRYICSIAE 2099
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 2269-2406 1.50e-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: 84.21  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2269 RNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYesknrgiYMFRLD----EDRVVDATLSGGLAR 2344
Cdd:cd10535   90 RARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS-------YLFDLDnkdgEVYCIDARFYGNVSR 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24639197 2345 YINHSCNPNCVTEIVEVD----RDVRIIIFAKRKIYRGEELSYDYK---FDIEDEShkIPCACGAPNCR 2406
Cdd:cd10535  163 FINHHCEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYGerfWDIKGKL--FSCRCGSPKCR 229
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 1902-1963 3.04e-17

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: 78.52  E-value: 3.04e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24639197 1902 WVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNSLYHLPCA 1963
Cdd:cd15665   10 YAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCA 71
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
 1902-1981 4.41e-17

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: 78.80  E-value: 4.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1902 WVHLNCALWSNGVYeTVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNSLYHLPCAIREECVFYK-NKSVHCSV 1980
Cdd:cd15699   24 WVHEGCILWANGIY-LVCGRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLNEeNFSVRCPK 102


                 .
gi 24639197 1981 H 1981
Cdd:cd15699  103 H 103
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 2274-2406 1.96e-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: 81.22  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2274 LARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYesknrgiYMFRLD----EDRVVDATLSGGLARYINHS 2349
Cdd:cd10533   95 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDS-------YLFDLDnkdgEVYCIDARYYGNISRFINHL 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24639197 2350 CNPNCV-TEIVEVDRDV---RIIIFAKRKIYRGEELSYDYK---FDIedESHKIPCACGAPNCR 2406
Cdd:cd10533  168 CDPNIIpVRVFMLHQDLrfpRIAFFSSRDIRTGEELGFDYGdrfWDI--KSKYFTCQCGSEKCK 229
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 2283-2388 4.67e-16

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


Pssm-ID: 380927  Cd Length: 127  Bit Score: 76.54  E-value: 4.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2283 GLYAARDIEKHTMIIEYIGEV-IRTEVseirEKQYESKNRG---IYMFRLDEDR--VVDATLSGGLARYINHSCNPNCVT 2356
Cdd:cd10529   18 GLVATEDISPGEPILEYKGEVsLRSEF----KEDNGFFKRPspfVFFYDGFEGLplCVDARKYGNEARFIRRSCRPNAEL 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 24639197 2357 EIVEVDRD-VRIIIFAKRKIYRGEELSYDYKFD 2388
Cdd:cd10529   94 RHVVVSNGeLRLFIFALKDIRKGTEITIPFDYD 126
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 2281-2407 5.29e-16

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


Pssm-ID: 380915 [Multi-domain]  Cd Length: 288  Bit Score: 80.80  E-value: 5.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2281 GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQY-----------ESknrgIYMFRLDEDR-------VVDATLSGGL 2342
Cdd:cd10517  140 GWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYgdeyfaeldyiEV----VEKLKEGYESdveehcyIIDAKSEGNL 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2343 ARYINHSCNPNCVTEIVEVD-RDVR---IIIFAKRKIYRGEELSYDYKFDI-EDESHKIPCACGAPNCRK 2407
Cdd:cd10517  216 GRYLNHSCSPNLFVQNVFVDtHDLRfpwVAFFASRYIRAGTELTWDYNYEVgSVPGKVLYCYCGSSNCRG 285
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 1902-1981 9.69e-16

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: 74.91  E-value: 9.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1902 WVHLNCALWSNGVYeTVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNSLYHLPCAIREECVFY-KNKSVHCSV 1980
Cdd:cd15700   25 WVHEACAVWTTGVY-LVAGKLFGLQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEeENFSLRCPK 103


                 .
gi 24639197 1981 H 1981
Cdd:cd15700  104 H 104
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 2282-2396 1.16e-14

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: 73.98  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2282 LGLYAARDIEKHTMIIEYIGEVIRtevseirEKQYESKNRGIY----------MFRLDEDRVVDATLSGGLARYINHSCN 2351
Cdd:cd19183   14 FGLFADRPIPAGDPIQELLGEIGL-------QSEYIADPENQYqilgapkphvFFHPQSPLYIDTRRSGSVARFIRRSCR 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 24639197 2352 PNCVTEIVEVD--RDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKI 2396
Cdd:cd19183   87 PNAELVTVASDsgSVLKFVLYASRDISPGEEITIGWDWDNPHPFRRF 133
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 1877-1981 4.25e-14

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


Pssm-ID: 277139 [Multi-domain]  Cd Length: 112  Bit Score: 70.36  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNqRGDGQADGPSRLLNFDvDKWVHLNCALWSNGVYE--TVSGALMNF-----QTALQAGLSQACSACHQPGATIKC 1949
Cdd:cd15669    1 CVLCG-RSDDDPDKYGEKLQKD-GICAHYFCLLFSSGLPQrgEDNEGIYGFlpediRKEVRRASRLRCFYCKKKGASIGC 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 24639197 1950 FKSRCNSLYHLPCAIREECV--FYKNKSVHCSVH 1981
Cdd:cd15669   79 AVKGCRRSFHFPCGLENGCVtqFFGEYRSFCWEH 112
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 1900-1963 6.51e-14

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


Pssm-ID: 277166  Cd Length: 90  Bit Score: 69.20  E-value: 6.51e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24639197 1900 DKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNSLYHLPCA 1963
Cdd:cd15696    8 ECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 71
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 2274-2407 8.43e-14

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: 73.35  E-value: 8.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2274 LARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSE----IREKQYESKNRGIYmfrlDEDRVVDATLSGGLARYINHS 2349
Cdd:cd10541   96 LFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADkeglEMGDEYFANLDHIE----ESCYIIDAKLEGNLGRYLNHS 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2350 CNPNCVTEIVEVD-RDVR---IIIFAKRKIYRGEELSYDYKFDIED-ESHKIPCACGAPNCRK 2407
Cdd:cd10541  172 CSPNLFVQNVFVDtHDLRfpwVAFFASKRIKAGTELTWDYNYEVGSvEGKELLCCCGSNECRG 234
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 2280-2409 1.19e-13

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


Pssm-ID: 380921 [Multi-domain]  Cd Length: 266  Bit Score: 73.71  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2280 QGLGLYAARDIEKHTMIIEYIGEV-IRT-----------------EVSEIREKQYESKNRGiymfRLDEDRVVDATLSGG 2341
Cdd:cd10523  118 KGWGVRCLDDIDKGTFVCIYAGRVlSRArspteplppklelpsenEVEVVTSWLILSKKRK----LRENVCFLDASKEGN 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2342 LARYINHSCNPNCVTEIVEVDRDVR----IIIFAKRKIYRGEELSYDYKFDIEDESHK-IPCACGAPNCRKWM 2409
Cdd:cd10523  194 VGRFLNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYSYDAGTSPEQeIPCLCGVNKCQKKI 266
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 1899-1963 3.38e-13

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


Pssm-ID: 277165  Cd Length: 90  Bit Score: 67.25  E-value: 3.38e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24639197 1899 VDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNSLYHLPCA 1963
Cdd:cd15695    7 GECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCA 71
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 1904-1981 2.83e-12

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: 64.66  E-value: 2.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   1904 HLNCALWSNGVY--ETVSGA--LMNFQTALQAGLSQACSACHQP-GATIKCFKSRCNSLYHLPCAIREECVF-YKNKSV- 1976
Cdd:pfam13771    1 HVVCALWSPELVqrGNDSMGfpIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDNGt 80


                   ....*...
gi 24639197   1977 ---HCSVH 1981
Cdd:pfam13771   81 fksYCKKH 88
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
1875-1981 1.72e-11

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 63.13  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   1875 RQCVFCNQRGDGqadgpsrLLNFDVDKWVHLNCALW----SNGVYETVSgaLMNFQTALQAGLSQACSACHQP-GATIKC 1949
Cdd:pfam13832    1 VRCCLCPLRGGA-------LKQTSDGRWVHVLCAIFvpevRFGNVATME--PIDVSRIPPERWKLKCVFCKKRsGACIQC 71

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 24639197   1950 FKSRCNSLYHLPCAIRE------ECVFYKNKSVHCSVH 1981
Cdd:pfam13832   72 SKGRCTTAFHVTCAQAAgvymepEDWPNVVVIAYCQKH 109
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
 1877-1981 5.06e-11

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: 62.02  E-value: 5.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGQADGPSRLLNFDVDkwVHLNCALWSNGVYETVSGALMNF--------QTALQAGLSQACSACHQPGATIK 1948
Cdd:cd15673    1 CGFCKSGEENKETGGKLASGEKIA--AHHNCMLFSSGLVQYVSPNENDFggfdiedvKKEIKRGRKLKCNLCKKTGATIG 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 24639197 1949 CFKSRCNSLYHLPCAIREECVFYKNKS-----VHCSVH 1981
Cdd:cd15673   79 CDVKQCKKTYHYHCAKKDDAKIIERNSqgiyrVYCKNH 116
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 2269-2385 3.13e-10

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: 62.81  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2269 RNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYE--------SKNRGI-YMFRLDEDR------- 2332
Cdd:cd10545   85 RYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDDylfdidnrQTNRGWdGGQRLDVGMsdgerss 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24639197 2333 ---------VVDATLSGGLARYINHSCNPNCVTEIVEVD----RDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd10545  165 aedeessefTIDAGSFGNVARFINHSCSPNLFVQCVLYDhndlRLPRVMLFAADNIPPLQELTYDY 230
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 2284-2405 2.77e-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: 58.10  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2284 LYAARDIEKHTMIIEYIGEVIRTEVSEIR----EKQYE-----SKNRGIYMfrldedrVVDATLSGGLARYINHSCNPNC 2354
Cdd:cd19181   21 LRAARDLALDTLIIEYRGKVMLRQQFEVNghffKRPYPfvlfySKFNGVEM-------CVDARTFGNDARFIRRSCTPNA 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24639197 2355 VTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCAC--GAPNC 2405
Cdd:cd19181   94 EVRHMIADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCAChkGNRNC 146
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 2281-2385 4.43e-09

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: 56.62  E-value: 4.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2281 GLGLYAARDIEKhtmiieyiGEVIRTE------VSEIREKQYESKNRGIYMFRLdedrvvdatlsgglARYINHSCNPNC 2354
Cdd:cd20071   10 GRGLVATRDIEP--------GELILVEkplvsvPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA 67

                         90       100       110
                 ....*....|....*....|....*....|.
gi 24639197 2355 VteiVEVDRDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd20071   68 V---VVFDGNGTLRVRALRDIKAGEELTISY 95
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 2271-2400 6.63e-07

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: 50.74  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2271 NVYLARSKiQGLGLYAARDIEKHTMIIEYIGEVIrtEVSEIREKQYESKNRG---IYMFRLDEDRVVDatlsgGLARYIN 2347
Cdd:cd10524   10 NRYSLENH-YGAKIIATKPIKKGEKIHELCGCIA--ELSEEEEALLRPGGNDfsvMYSSRKKCSQLWL-----GPAAFIN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24639197 2348 HSCNPNCvtEIVEVDRDvRIIIFAKRKIYRGEELSYDY--KFDIEDESHkipCAC 2400
Cdd:cd10524   82 HDCRPNC--KFVPTGKS-TACVKVLRDIEPGEEITVYYgdNYFGENNEE---CEC 130
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 1877-1981 7.10e-07

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: 49.96  E-value: 7.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCnqRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVY------ETVSG-ALMNFQTALQAGLSQACSACHQPGATIKC 1949
Cdd:cd15710    1 CGFC--RSNREKECGQLLISENQKVAAHHKCMLFSSALVsshsdsENLGGfSIEDVQKEIKRGTKLMCSLCHCPGATIGC 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 24639197 1950 FKSRCNSLYHLPCAIREECVFYKNKS-----VHCSVH 1981
Cdd:cd15710   79 DVKTCHRTYHYYCALHDKAQIRENPSqgiymIYCRKH 115
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
 2284-2388 7.14e-07

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: 50.28  E-value: 7.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2284 LYAARDIEKHTMIIEYIGEVIRTEVSEIR----EKQYE-----SKNRGIYMfrldedrVVDATLSGGLARYINHSCNPNC 2354
Cdd:cd19182   21 LKAAKDLPPDTLIIEYRGKFMLREQFEANgyffKRPYPfvlfySKFHGLEM-------CVDARTFGNEARFIRRSCTPNA 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 24639197 2355 VTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFD 2388
Cdd:cd19182   94 EVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFD 127
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 1877-1981 1.09e-06

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: 49.70  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQrGDGQADGPSRLLNFDVDK-WVHLNCALWSNGVYETVSGALMNF-----QTALQA---GLSQACSACHQPGATI 1947
Cdd:cd15711    1 CGFCHA-GEEENETRGKLHIFNAKKaAAHYKCMLFSSGTVQLTTTSRAEFgdfdiKTVIQEikrGKRMKCTLCSQLGATI 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 24639197 1948 KCFKSRCNSLYHLPCAIREECVFYKNKS-----VHCSVH 1981
Cdd:cd15711   80 GCEIKACVKTYHYHCGVQDKAKYIENMSrgiykLYCKNH 118
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
 2280-2385 2.78e-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: 48.95  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2280 QGLGLYAARDIEKHTMIIEYIGEVirtevSEIREKQYEsKNRGIYMFRLDEDR----VVDATLSGGLARYI----NHS-- 2349
Cdd:cd10539   14 EGFTVEADGFIKDLTIIAEYTGDV-----DYIRNREFD-DNDSIMTLLLAGDPskslVICPDKRGNIARFIsginNHTkd 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 24639197 2350 ----CNPNCVTeiVEVDRDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd10539   88 gkkkQNCKCVR--YSINGEARVLLVATRDIAKGERLYYDY 125
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
 1877-1977 3.21e-05

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: 45.40  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCnqrgdgqadgPSRLLNF---DVDKWVHLNCALW------SNGVY-ETVsgalMNFQTALQAGLSQACSACHQP-GA 1945
Cdd:cd15670    1 CVLC----------PNKGGAFkqtDDGRWAHVVCALWipevsfANTVFlEPI----DGIQNIPKARWKLTCYICKKRmGA 66

                         90       100       110
                 ....*....|....*....|....*....|..
gi 24639197 1946 TIKCFKSRCNSLYHLPCAiREECVFYKNKSVH 1977
Cdd:cd15670   67 CIQCHKKNCYTAFHVTCA-QQAGLYMKIEPVK 97
ePHD_PHF14 cd15674
Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended ...
 1898-1966 4.29e-05

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: 45.07  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1898 DVDKWVHLNCALWSNGV-------YETVSGALMNFQTAlqagLSQACSACHQP-----GATIKCFKSRCNSLYHLPCAIR 1965
Cdd:cd15674   15 DTGRWVHLVCALYTPGVafgdvdkLSPVTLTEMNYSKW----GARECSLCEDPrfartGVCISCDAGMCKSYFHVTCAQR 90


                 .
gi 24639197 1966 E 1966
Cdd:cd15674   91 E 91
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 2272-2391 6.67e-05

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: 44.17  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2272 VYLARSKIQGLGLYAARDIEKhtmiieyiGEVIrtEVS---EIREKQY---ESKNRGIYMFRLDEDRVVDATLSGGLAry 2345
Cdd:cd10540    2 LEVKPSTLKGRGVFATRPIKK--------GEVI--EEApviVLPKEEYqhlCKTVLDHYVFSWGDGCLALALGYGSMF-- 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 24639197 2346 iNHSCNPNcvteiVEVDRDV---RIIIFAKRKIYRGEELSYDYKFDIED 2391
Cdd:cd10540   70 -NHSYTPN-----AEYEIDFenqTIVFYALRDIEAGEELTINYGDDLWD 112
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 1903-1969 9.26e-05

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: 44.12  E-value: 9.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24639197 1903 VHLNCALWSNGVYET---------VSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNSLYHLPCAIREECV 1969
Cdd:cd15712   23 AHQNCLLYSSGFVESeeynplnldRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALCDDAA 98
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
 1877-1981 9.84e-05

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: 9.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGqadgpsrLLNFDVDKWVHLNCALW------SNGVY-ETVSGAlmnfQTALQAGLSQACSACHQP--GATI 1947
Cdd:cd15702    1 CVLCPNKGGA-------FKKTDDDRWGHVVCALWipevgfANTVFiEPIDGV----RNIPPARWKLTCYLCKQKgvGACI 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 24639197 1948 KCFKSRCNSLYHLPCA-----------IRE----ECVFYKNKSVHCSVH 1981
Cdd:cd15702   70 QCHKANCYTAFHVTCAqkaglymkmepVKEvtggGTTFSVRKTAYCDAH 118
PRK13914 PRK13914
invasion associated endopeptidase;
602-830 1.17e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 47.10  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   602 VLSKTTMAQQKPKMITTTTLSSQAA---LQMHHALIQDSSADKAGSSANSGSATSGASMQlKLTTANTPTKLSVSLAPDV 678
Cdd:PRK13914  143 VTSTPVAPTQEVKKETTTQQAAPAAetkTEVKQTTQATTPAPKVAETKETPVVDQNATTH-AVKSGDTIWALSVKYGVSV 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   679 VKLEEVGSESKAKLLVKQEAVVKDS--TGTPTSEER-----AEEIGTPEKRLNANATMTAinQVQNQSANQIQMATSTST 751
Cdd:PRK13914  222 QDIMSWNNLSSSSIYVGQKLAIKQTanTATPKAEVKteapaAEKQAAPVVKENTNTNTAT--TEKKETTTQQQTAPKAPT 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   752 ASNPSTPNPTV----NATPMNNQRSAAEDNALLKQLLQNNSSSHSLNQISITSAHVGSASASAPLSARKVINVRAPSMGK 827
Cdd:PRK13914  300 EAAKPAPAPSTntnaNKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASAIIAEAQKHLGK 379


                  ...
gi 24639197   828 VRS 830
Cdd:PRK13914  380 AYS 382
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 1877-1966 1.45e-04

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: 43.20  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDgqADGPSRllnfDVDKWVHLNCALW----SNGVYETVSgALMNFQTALQAGLSQACSACH-QPGATIKCFK 1951
Cdd:cd15671    1 CVLCPKKGG--AMKSTK----SGTKWVHVSCALWipevSIGCPEKME-PITKISHIPMSRWALVCVLCKeKTGACIQCSV 73

                         90
                 ....*....|....*
gi 24639197 1952 SRCNSLYHLPCAIRE 1966
Cdd:cd15671   74 KSCKTAFHVTCAFQH 88
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
 1877-1965 2.12e-04

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: 43.12  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDG---QADGpsrllnfdvdKWVHLNCALW------SNGVY-ETVSGAlmnfQTALQAGLSQACSACHQP--G 1944
Cdd:cd15703    1 CVLCPNKGGAfkqTSDG----------RWAHVVCAIWipevcfANTVFlEPVEGV----NNIPPARWKLTCYLCKQKgrG 66

                         90       100
                 ....*....|....*....|.
gi 24639197 1945 ATIKCFKSRCNSLYHLPCAIR 1965
Cdd:cd15703   67 AAIQCHKVNCYTAFHVTCAQR 87
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
 1877-1963 2.63e-04

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: 42.78  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDgqADGPSRllnfDVDKWVHLNCALW----SNGVYETVSgALMNFQTALQAGLSQACSACHQ-PGATIKCFK 1951
Cdd:cd15705    1 CLLCPKRGG--ALKPTR----SGTKWVHVSCALWipevSIGCPEKME-PITKISHIPASRWALSCSLCKEcTGTCIQCSM 73

                         90
                 ....*....|..
gi 24639197 1952 SRCNSLYHLPCA 1963
Cdd:cd15705   74 PSCITAFHVTCA 85
ePHD_Snt2p_like cd15667
Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) ...
 1877-1963 2.89e-04

Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Snt2p. Sntp2 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 PHD fingers, a non-canonical ePHD finger, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain.


Pssm-ID: 277137  Cd Length: 141  Bit Score: 43.14  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRG---DGQADGPSRLLN-----FDVDKWVHLNCALWSNGVyETVSGALM----NFQTALQAGLSQACSACHQP- 1943
Cdd:cd15667    1 CSLCNAKEsnyELAKKQSPRTRPdalkcTSNGTWCHVLCALFNEDI-KFGNSKSLqpilNTESVLLKGSRQKCEICKVSg 79

                         90       100
                 ....*....|....*....|
gi 24639197 1944 GATIKCfkSRCNSLYHLPCA 1963
Cdd:cd15667   80 GGLVKC--EVCDDRFHVSCA 97
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 1937-1981 2.94e-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: 2.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24639197 1937 CSACHQPG----ATIKCfkSRCNSLYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:cd15489    2 CIVCGKGGdlggELLQC--DGCGKWFHADCLGPPLSSFVPNGKWICPVC 48
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 2272-2385 7.85e-04

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: 41.52  E-value: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 2272 VYLARSKIQ--GLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESknrgiYMFRLDEDRVVDATL--------SGG 2341
Cdd:cd10530    9 VYVAESLIPsaGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNG-----NTISLDEETVIDVPEpynsvskyCAS 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 24639197 2342 LARYINHSCNPNCVTEIVEVDRDVRI-IIFAKRKIYRGEELSYDY 2385
Cdd:cd10530   84 LGHKANHSFTPNCIYDPFVHPRFGPIkCIRTLRAVEAGEELTVAY 128
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
1875-1977 9.50e-04

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 44.59  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1875 RQCVFCnqrgdgqadgPSRLLNF---DVDKWVHLNCALWSNGVY--ETVSGALMNFQTALQAGLSQA-CSACHQPGAT-I 1947
Cdd:COG5141  248 RCCSFC----------PSSDGAFkqtSDGRWGHVICAMFNPELSfgHLLSKDPIDNIASVSSSRWKLgCLICKEFGGTcI 317

                         90       100       110
                 ....*....|....*....|....*....|
gi 24639197 1948 KCFKSRCNSLYHLPCAiREECVFYKNKSVH 1977
Cdd:COG5141  318 QCSYFNCTRAYHVTCA-RRAGYFDLNIYSH 346
PostSET smart00508
Cysteine-rich motif following a subset of SET domains;
2394-2410 1.24e-03

Cysteine-rich motif following a subset of SET domains;


Pssm-ID: 214703  Cd Length: 17  Bit Score: 38.16  E-value: 1.24e-03
                            10
                    ....*....|....*..
gi 24639197    2394 HKIPCACGAPNCRKWMN 2410
Cdd:smart00508    1 KKQPCLCGAPNCRGFLG 17
PHA03255 PHA03255
BDLF3; Provisional
 124-299 1.86e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.20  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   124 SGTEMGAIKAEDADKQTFTSFTKKEGASSSASSSSSTASVISIEPSGSGQDHAENSGKSEDLDYVLMPASGADSSTSVGN 203
Cdd:PHA03255    4 ARDKAGAVLAMILICETSLIWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197   204 STGTGTPAGTPIGATTSTIILN--ANNGTAGVSGAGTTTILTQKSghtnynifNTTATGSQTPTTTLLNRVNLHPKMktq 281
Cdd:PHA03255   84 TGTTVTPVPTTSNASTINVTTKvtAQNITATEAGTGTSTGVTSNV--------TTRSSSTTSATTRITNATTLAPTL--- 152

                         170
                  ....*....|....*...
gi 24639197   282 lmvNAKKLSEVTQTTAKV 299
Cdd:PHA03255  153 ---SSKGTSNATKTTAEL 167
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1937-1981 2.42e-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: 37.96  E-value: 2.42e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 24639197    1937 CSACHQP---GATIKCfkSRCNSLYHLPCAIREECVFYKNKSVHCSVH 1981
Cdd:smart00249    2 CSVCGKPddgGELLQC--DGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 2336-2385 4.56e-03

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


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 41.13  E-value: 4.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24639197 2336 ATLSgglarYINHSCNPNCVTEIVevdrDVRIIIFAKRKIYRGEELSYDY 2385
Cdd:cd10536  149 PTLS-----LLNHSCDPNTIRSFY----GNTIVVRATRPIKKGEEITICY 189
ePHD_BRPF1 cd15701
Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...
 1877-1981 5.96e-03

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: 38.91  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1877 CVFCNQRGDGqadgpsrLLNFDVDKWVHLNCALW------SNGVYETVSGALMNFQTALqagLSQACSACHQ--PGATIK 1948
Cdd:cd15701    1 CALCPNKGGA-------FKQTDDGRWAHVVCALWipevcfANTVFLEPIDSIEHIPPAR---WKLTCYICKQrgSGACIQ 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 24639197 1949 CFKSRCNSLYHLPCA-----------IREECV----FYKNKSVHCSVH 1981
Cdd:cd15701   71 CHKANCYTAFHVTCAqqaglymkmepVRETGAngtsFSVRKTAYCDIH 118
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
 1876-1963 9.33e-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: 38.51  E-value: 9.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639197 1876 QCVFCNQRGDgqADGPSRllnfDVDKWVHLNCALW----SNGVYETVSgALMNFQTALQAGLSQACSACHQP-GATIKCF 1950
Cdd:cd15704    3 KCLLCPKKGG--AMKPTR----SGTKWVHVSCALWipevSIGSPEKME-PITKVSHIPSSRWALVCSLCNEKvGASIQCS 75

                         90
                 ....*....|...
gi 24639197 1951 KSRCNSLYHLPCA 1963
Cdd:cd15704   76 VKNCRTAFHVTCA 88
 
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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