NCBI Conserved Domain Search

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

4450-4554

4.95e-74

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: 242.26 E-value: 4.95e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15697     1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                          90       100
                  ....*....|....*....|....*
gi 578814480 4530 IYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:cd15697    81 VYHFTCAIKAQCMFFKDKTMLCPMH 105

ePHD1_KMT2C

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

248-331

3.33e-55

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: 187.84 E-value: 3.33e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  248 GTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLL 327
Cdd:cd15696     7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86


                  ....
gi 578814480  328 CPEH 331
Cdd:cd15696    87 CPTH 90

HMG-box_KMT2C

cd22026

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...

1650-1730

2.63e-54

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C, also called 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.

Pssm-ID: 438835 Cd Length: 81 Bit Score: 184.99 E-value: 2.63e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1650 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 1729
Cdd:cd22026     1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80


                  .
gi 578814480 1730 N 1730
Cdd:cd22026    81 N 81

PHD4_KMT2C

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

953-1009

8.51e-37

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

Pssm-ID: 277071 Cd Length: 57 Bit Score: 134.37 E-value: 8.51e-37

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480  953 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 1009
Cdd:cd15596     1 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 57

PHD6_KMT2C

cd15600

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1087-1137

2.12e-32

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

Pssm-ID: 277073 Cd Length: 51 Bit Score: 121.58 E-value: 2.12e-32

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1087 SCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVADIGFDCSMC 1137
Cdd:cd15600     1 TCPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC 51

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

1010-1056

1.95e-30

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

Pssm-ID: 276988 Cd Length: 47 Bit Score: 115.65 E-value: 1.95e-30

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1056
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

PHD2_KMT2C

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

391-436

5.40e-29

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

Pssm-ID: 277069 Cd Length: 46 Bit Score: 111.57 E-value: 5.40e-29

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15594     1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

PHD3_KMT2C

cd15511

PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

467-518

8.50e-28

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

Pssm-ID: 276986 Cd Length: 52 Bit Score: 108.34 E-value: 8.50e-28

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  467 LCPFCGKCYHPELQKDMLHCNMCKRWVHLECDKPTDHELDTQLKEEYICMYC 518
Cdd:cd15511     1 PCPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

4658-4745

2.60e-24

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: 99.68 E-value: 2.60e-24

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   4658 VFVIRIVEQGheDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENYTF 4737
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78


                    ....*...
gi 578814480   4738 RYGRNPLM 4745
Cdd:smart00542   79 RYHRSPLL 86

PHA03247 super family

cl33720

large tegument protein UL36; Provisional

1893-2370

5.64e-24

large tegument protein UL36; Provisional

The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 112.72 E-value: 5.64e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1893 PPSPQVFSPGSSNSRPPSPMdpYAkmvgtPRPP-PVGHSFSRRNSAAPvENCTPLSSVSRPLQMNETTANRPSPvrdlcs 1971
Cdd:PHA03247 2553 PPLPPAAPPAAPDRSVPPPR--PA-----PRPSePAVTSRARRPDAPP-QSARPRAPVDDRGDPRGPAPPSPLP------ 2618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1972 ssttnndPYAKPPDTPRPvmtdqfpkslglSRSPVVSEQTAKGPIAAGTSDHFTK-PSPRAdvFQRQRIPDSYARPlltp 2050
Cdd:PHA03247 2619 -------PDTHAPDPPPP------------SPSPAANEPDPHPPPTVPPPERPRDdPAPGR--VSRPRRARRLGRA---- 2673

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2051 apldsgPGPFKTPMQP-PPSSQDPYGSVSQASRRLSVDPYERPA------LTPRPIDNFSHNQSNDPYSQPPLTPHPAVN 2123
Cdd:PHA03247 2674 ------AQASSPPQRPrRRAARPTVGSLTSLADPPPPPPTPEPAphalvsATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2124 ESFAHPSRAFSQPGTISRPTSQDPYSQPPGTP-----RPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQTP 2198
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP 2827

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2199 RPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPGISV----PYSQPPATP----RPRIsegftrSSMTRPVLMPNQDPFLQA 2270
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVrrrpPSRSPAAKPaapaRPPV------RRLARPAVSRSTESFALP 2901

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2271 A-------QNRGPALPGPLVRPPDTCSQTPRPPGPGLSDT--FSRVSPSAARDPYDQSPmTPRSQSDSFGTSQTAHDVAD 2341
Cdd:PHA03247 2902 PdqperppQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPplAPTTDPAGAGEPSGAVP-QPWLGALVPGRVAVPRFRVP 2980

                         490       500
                  ....*....|....*....|....*....
gi 578814480 2342 QPRPGSEGSfcASSNSPMHsqGQQFSGVS 2370
Cdd:PHA03247 2981 QPAPSREAP--ASSTPPLT--GHSLSRVS 3005

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

344-389

8.99e-24

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

Pssm-ID: 276984 Cd Length: 48 Bit Score: 96.61 E-value: 8.99e-24

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480  344 NCAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAV--TPLKRAGWQCPEC 389
Cdd:cd15509     1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48

FYRN

pfam05964

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

4599-4650

4.70e-18

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: 80.63 E-value: 4.70e-18

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  4599 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 4650
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

Atrophin-1 super family

cl38111

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

2236-2564

1.35e-05

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

The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.69 E-value: 1.35e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2236 SQPPATPRPRISEGFTRSSMTRPVLMpNQDPFLQAAQnrGPALPGPLVRPPDTCSQTPRPPgPGLSDTFSRVSPSAARDP 2315
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQ-TQPPVLQAQS--GAASPPSPPPPGTTQAATAGPT-PSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2316 YDQSPM---------TPRSQSDSFGTSQTAHDVADQPRPGSEGSFCASSNSPMHSQGQQF-----SGVSQLPGPVPTSGV 2381
Cdd:pfam03154  219 NQTQSTaaphtliqqTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMphslqTGPSHMQHPVPPQPF 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2382 TDTQntvNMAQADTEKLRQRQklreiilqqQQQKKIAGRQEKGSQDSPAVPHPGPLQHWQPENVNQAFTRPPPPYP---- 2457
Cdd:pfam03154  299 PLTP---QSSQSQVPPGPSPA---------APGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPipql 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2458 GNIRSPVAPPLGPRYAVFPKDQRGPYPPDVASMGMRPHgfrfGFPGGSH----GTMPSQERFLVPPQQIQGSGVSPQLRR 2533
Cdd:pfam03154  367 PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLST----HHPPSAHppplQLMPQSQQLPPPPAQPPVLTQSQSLPP 442

                          330       340       350
                   ....*....|....*....|....*....|..
gi 578814480  2534 SVSvDMPRPLNNSQMNNPVGLPQH-FSPQSLP 2564
Cdd:pfam03154  443 PAA-SHPPTSGLHQVPSQSPFPQHpFVPGGPP 473

TPH super family

cl38442

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

3193-3289

3.36e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.

The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 3.36e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  3193 QRKQ--YEEWLQETQQLLQMQQKYLEEQigahrksKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQIRK 3270
Cdd:pfam13868   87 QKRQeeYEEKLQEREQMDEIVERIQEED-------QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159

                           90
                   ....*....|....*....
gi 578814480  3271 QQKEHAELIEDYRIKQQQQ 3289
Cdd:pfam13868  160 YLKEKAEREEEREAEREEI 178

Name

Accession

Description

Interval

E-value

SET_KMT2C_2D

cd19171

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

4806-4958

1.75e-117

Pssm-ID: 380948 [Multi-domain] Cd Length: 153 Bit Score: 368.68 E-value: 1.75e-117

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4806 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 4885
Cdd:cd19171     1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4886 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4958
Cdd:cd19171    81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153

ePHD2_KMT2C

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

4450-4554

4.95e-74

Pssm-ID: 277167 Cd Length: 105 Bit Score: 242.26 E-value: 4.95e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15697     1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                          90       100
                  ....*....|....*....|....*
gi 578814480 4530 IYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:cd15697    81 VYHFTCAIKAQCMFFKDKTMLCPMH 105

ePHD1_KMT2C

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

248-331

3.33e-55

Pssm-ID: 277166 Cd Length: 90 Bit Score: 187.84 E-value: 3.33e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  248 GTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLL 327
Cdd:cd15696     7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86


                  ....
gi 578814480  328 CPEH 331
Cdd:cd15696    87 CPTH 90

HMG-box_KMT2C

cd22026

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...

1650-1730

2.63e-54

Pssm-ID: 438835 Cd Length: 81 Bit Score: 184.99 E-value: 2.63e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1650 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 1729
Cdd:cd22026     1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80


                  .
gi 578814480 1730 N 1730
Cdd:cd22026    81 N 81

SET

COG2940

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

4818-4957

2.01e-38

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 141.64 E-value: 2.01e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgvYMFRMDNDHVIDATLTGGPARYINH 4897
Cdd:COG2940     5 HPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4898 SCAPNCVAEvvtfERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHkiPCHCGavNCRKW 4957
Cdd:COG2940    83 SCDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134

PHD4_KMT2C

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

953-1009

8.51e-37

Pssm-ID: 277071 Cd Length: 57 Bit Score: 134.37 E-value: 8.51e-37

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480  953 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 1009
Cdd:cd15596     1 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 57

SET

smart00317

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

4820-4941

1.05e-35

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: 133.61 E-value: 1.05e-35

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   4820 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNR-GVYMFRMDNDHVIDATLTGGPARYINHS 4898
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHS 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 578814480   4899 CAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDD 4941
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

PHD6_KMT2C

cd15600

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1087-1137

2.12e-32

Pssm-ID: 277073 Cd Length: 51 Bit Score: 121.58 E-value: 2.12e-32

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1087 SCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVADIGFDCSMC 1137
Cdd:cd15600     1 TCPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC 51

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

1010-1056

1.95e-30

Pssm-ID: 276988 Cd Length: 47 Bit Score: 115.65 E-value: 1.95e-30

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1056
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

SET

pfam00856

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

4830-4935

1.99e-29

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: 115.31 E-value: 1.99e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  4830 GLGLYAARDIEKHTMVIEYIGT-IIRNEVANRKEKLYESQNR----GVYMFRMDND--HVIDATLT--GGPARYINHSCA 4900
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARALyyGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 578814480  4901 PNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYK 4935
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

PHD2_KMT2C

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

391-436

5.40e-29

Pssm-ID: 277069 Cd Length: 46 Bit Score: 111.57 E-value: 5.40e-29

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15594     1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

PHD3_KMT2C

cd15511

PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

467-518

8.50e-28

Pssm-ID: 276986 Cd Length: 52 Bit Score: 108.34 E-value: 8.50e-28

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  467 LCPFCGKCYHPELQKDMLHCNMCKRWVHLECDKPTDHELDTQLKEEYICMYC 518
Cdd:cd15511     1 PCPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

4658-4745

2.60e-24

Pssm-ID: 197781 Cd Length: 86 Bit Score: 99.68 E-value: 2.60e-24

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   4658 VFVIRIVEQGheDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENYTF 4737
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78


                    ....*...
gi 578814480   4738 RYGRNPLM 4745
Cdd:smart00542   79 RYHRSPLL 86

PHA03247

large tegument protein UL36; Provisional

1893-2370

5.64e-24

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 112.72 E-value: 5.64e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1893 PPSPQVFSPGSSNSRPPSPMdpYAkmvgtPRPP-PVGHSFSRRNSAAPvENCTPLSSVSRPLQMNETTANRPSPvrdlcs 1971
Cdd:PHA03247 2553 PPLPPAAPPAAPDRSVPPPR--PA-----PRPSePAVTSRARRPDAPP-QSARPRAPVDDRGDPRGPAPPSPLP------ 2618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1972 ssttnndPYAKPPDTPRPvmtdqfpkslglSRSPVVSEQTAKGPIAAGTSDHFTK-PSPRAdvFQRQRIPDSYARPlltp 2050
Cdd:PHA03247 2619 -------PDTHAPDPPPP------------SPSPAANEPDPHPPPTVPPPERPRDdPAPGR--VSRPRRARRLGRA---- 2673

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2051 apldsgPGPFKTPMQP-PPSSQDPYGSVSQASRRLSVDPYERPA------LTPRPIDNFSHNQSNDPYSQPPLTPHPAVN 2123
Cdd:PHA03247 2674 ------AQASSPPQRPrRRAARPTVGSLTSLADPPPPPPTPEPAphalvsATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2124 ESFAHPSRAFSQPGTISRPTSQDPYSQPPGTP-----RPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQTP 2198
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP 2827

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2199 RPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPGISV----PYSQPPATP----RPRIsegftrSSMTRPVLMPNQDPFLQA 2270
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVrrrpPSRSPAAKPaapaRPPV------RRLARPAVSRSTESFALP 2901

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2271 A-------QNRGPALPGPLVRPPDTCSQTPRPPGPGLSDT--FSRVSPSAARDPYDQSPmTPRSQSDSFGTSQTAHDVAD 2341
Cdd:PHA03247 2902 PdqperppQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPplAPTTDPAGAGEPSGAVP-QPWLGALVPGRVAVPRFRVP 2980

                         490       500
                  ....*....|....*....|....*....
gi 578814480 2342 QPRPGSEGSfcASSNSPMHsqGQQFSGVS 2370
Cdd:PHA03247 2981 QPAPSREAP--ASSTPPLT--GHSLSRVS 3005

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

344-389

8.99e-24

Pssm-ID: 276984 Cd Length: 48 Bit Score: 96.61 E-value: 8.99e-24

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480  344 NCAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAV--TPLKRAGWQCPEC 389
Cdd:cd15509     1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48

FYRC

pfam05965

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

4656-4740

1.11e-23

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

Pssm-ID: 461788 Cd Length: 83 Bit Score: 97.68 E-value: 1.11e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  4656 RPVFVIRIVEqgHEDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENY 4735
Cdd:pfam05965    1 GPLFRVTVEE--DPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78


                   ....*
gi 578814480  4736 TFRYG 4740
Cdd:pfam05965   79 KFRYG 83

FYRN

pfam05964

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

4599-4650

4.70e-18

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: 80.63 E-value: 4.70e-18

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  4599 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 4650
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

FYRN

smart00541

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...

4609-4652

1.47e-16

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: 76.17 E-value: 1.47e-16

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 578814480   4609 LLPQQMQAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSIEE 4652
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

4477-4554

2.49e-15

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: 73.90 E-value: 2.49e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  4477 HLNCALWSTEVYetQAGA------LINVELALRRGLQMKCVFCH-KTGATSGCHRFRCTNIYHFTCAIKAQCMF-FKDKT 4548
Cdd:pfam13771    1 HVVCALWSPELV--QRGNdsmgfpIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDN 78

                           90
                   ....*....|
gi 578814480  4549 ----MLCPMH 4554
Cdd:pfam13771   79 gtfkSYCKKH 88

PHD

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

1010-1056

1.01e-12

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

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 65.59 E-value: 1.01e-12

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 578814480  1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQT--VPKGGWKCKWCV 1056
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPaeIPSGEWLCPECK 49

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

253-331

5.38e-12

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 64.66 E-value: 5.38e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   253 HHRCVEWSLGVCQ-----MEEPLLvNVDKAVVSGSTERCAFCKH-LGATIKCCEEKCTQMYHYPCAAGAG---TFQDFSH 323
Cdd:pfam13771    1 HVVCALWSPELVQrgndsMGFPIE-DIEKIPKRRWKLKCYLCKKkGGACIQCSKKNCRRAFHVTCALEAGllmQFDEDNG 79


                   ....*....
gi 578814480   324 IFLL-CPEH 331
Cdd:pfam13771   80 TFKSyCKKH 88

PHD

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

1010-1055

1.38e-11

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: 62.23 E-value: 1.38e-11

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578814480   1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQT-VPKGGWKCKWC 1055
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD

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

391-439

3.12e-11

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 61.35 E-value: 3.12e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578814480   391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPV--MKSVPTNGWKCKNCRIC 439
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPldPAEIPSGEWLCPECKPK 51

Atrophin-1

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

2027-2382

2.72e-10

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 67.10 E-value: 2.72e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2027 PSPRADvfqrQRIPDSYARP--LLTPAPLDSGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDnfsh 2104
Cdd:pfam03154  149 PSPQDN----ESDSDSSAQQqiLQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQ---- 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2105 nqsndpySQPPLTPHPAVNESFA-HPSRAFS-----QPGTISRPTSQDPysqPPGTPRPVVDSYSQSSGTARSNTDPYSQ 2178
Cdd:pfam03154  221 -------TQSTAAPHTLIQQTPTlHPQRLPSphpplQPMTQPPPPSQVS---PQPLPQPSLHGQMPPMPHSLQTGPSHMQ 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2179 PPGTPRPTTVDPYSQQPQTP-RPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPG------ISVPYSQPP-ATPRPRISegf 2250
Cdd:pfam03154  291 HPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQplppapLSMPHIKPPpTTPIPQLP--- 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2251 TRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPGPGLSDTFSRVSPSAARDP-YDQSPMTPRSQSdS 2329
Cdd:pfam03154  368 NPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPvLTQSQSLPPPAA-S 446

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 578814480  2330 FGTSQTAHDVADQPrPGSEGSFCASSNSPMHS-QGQQFSGVSQLPGPVPTSGVT 2382
Cdd:pfam03154  447 HPPTSGLHQVPSQS-PFPQHPFVPGGPPPITPpSGPPTSTSSAMPGIQPPSSAS 499

PHD

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

391-436

2.88e-10

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 58.38 E-value: 2.88e-10

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578814480    391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKS-VPTNGWKCKNC 436
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD

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

961-1011

3.92e-10

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 58.27 E-value: 3.92e-10

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480   961 CVVCGsfGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKG-WRCLECTVC 1011
Cdd:pfam00628    2 CAVCG--KSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51

PHD

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

960-1008

5.22e-10

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 57.61 E-value: 5.22e-10

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 578814480    960 MCVVCGSFGqgAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLEC 1008
Cdd:smart00249    1 YCSVCGKPD--DGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

PHD

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

345-392

6.83e-09

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 54.42 E-value: 6.83e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 578814480   345 CAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAVT--PLKRAGWQCPECKVC 392
Cdd:pfam00628    2 CAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDpaEIPSGEWLCPECKPK 51

PHD

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

468-518

2.91e-07

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 49.90 E-value: 2.91e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 578814480    468 CPFCGKCYHPElqkDMLHCNMCKRWVHLECDKPTDHELDtqLKEEYICMYC 518
Cdd:smart00249    2 CSVCGKPDDGG---ELLQCDGCDRWYHQTCLGPPLLEEE--PDGKWYCPKC 47

PHD

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

345-389

5.30e-07

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 49.13 E-value: 5.30e-07

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578814480    345 CAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAVTP-LKRAGWQCPEC 389
Cdd:smart00249    2 CSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD

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

468-519

1.42e-06

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 47.87 E-value: 1.42e-06

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480   468 CPFCGKcyhPELQKDMLHCNMCKRWVHLECDKPTDhELDTQLKEEYICMYCK 519
Cdd:pfam00628    2 CAVCGK---SDDGGELVQCDGCDDWFHLACLGPPL-DPAEIPSGEWLCPECK 49

HMG_box

pfam00505

HMG (high mobility group) box;

1671-1722

1.29e-05

HMG (high mobility group) box;

Pssm-ID: 459837 [Multi-domain] Cd Length: 68 Bit Score: 45.68 E-value: 1.29e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 578814480  1671 VLYTNINFPNLKEEFPDWTTR--VKQIAKLWRKASSQERAPYVQKARDNRAALR 1722
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62

Atrophin-1

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

2236-2564

1.35e-05

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.69 E-value: 1.35e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2236 SQPPATPRPRISEGFTRSSMTRPVLMpNQDPFLQAAQnrGPALPGPLVRPPDTCSQTPRPPgPGLSDTFSRVSPSAARDP 2315
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQ-TQPPVLQAQS--GAASPPSPPPPGTTQAATAGPT-PSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2316 YDQSPM---------TPRSQSDSFGTSQTAHDVADQPRPGSEGSFCASSNSPMHSQGQQF-----SGVSQLPGPVPTSGV 2381
Cdd:pfam03154  219 NQTQSTaaphtliqqTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMphslqTGPSHMQHPVPPQPF 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2382 TDTQntvNMAQADTEKLRQRQklreiilqqQQQKKIAGRQEKGSQDSPAVPHPGPLQHWQPENVNQAFTRPPPPYP---- 2457
Cdd:pfam03154  299 PLTP---QSSQSQVPPGPSPA---------APGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPipql 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2458 GNIRSPVAPPLGPRYAVFPKDQRGPYPPDVASMGMRPHgfrfGFPGGSH----GTMPSQERFLVPPQQIQGSGVSPQLRR 2533
Cdd:pfam03154  367 PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLST----HHPPSAHppplQLMPQSQQLPPPPAQPPVLTQSQSLPP 442

                          330       340       350
                   ....*....|....*....|....*....|..
gi 578814480  2534 SVSvDMPRPLNNSQMNNPVGLPQH-FSPQSLP 2564
Cdd:pfam03154  443 PAA-SHPPTSGLHQVPSQSPFPQHpFVPGGPP 473

HMG

smart00398

high mobility group;

1669-1722

1.59e-05

high mobility group;

Pssm-ID: 197700 [Multi-domain] Cd Length: 70 Bit Score: 45.77 E-value: 1.59e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 578814480   1669 APVLYTNINFPNLKEEFPDWTT--RVKQIAKLWRKASSQERAPYVQKARDNRAALR 1722
Cdd:smart00398    8 AFMLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

3193-3289

3.36e-05

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 3.36e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  3193 QRKQ--YEEWLQETQQLLQMQQKYLEEQigahrksKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQIRK 3270
Cdd:pfam13868   87 QKRQeeYEEKLQEREQMDEIVERIQEED-------QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159

                           90
                   ....*....|....*....
gi 578814480  3271 QQKEHAELIEDYRIKQQQQ 3289
Cdd:pfam13868  160 YLKEKAEREEEREAEREEI 178

PHD

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

1088-1139

4.68e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 43.63 E-value: 4.68e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  1088 CPVCyRNYREEDLILQCRQCDRWMHAVCqnLNTEEEVENVADIGFDCSMCRP 1139
Cdd:pfam00628    2 CAVC-GKSDDGGELVQCDGCDDWFHLAC--LGPPLDPAEIPSGEWLCPECKP 50

FimV

COG3170

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];

2141-2471

5.74e-05

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];

Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 49.41 E-value: 5.74e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2141 RPTSQDPYSQPpgTPRPVVDSYSQSSGTARSNTDpYSQPPGTPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRhsDPY 2220
Cdd:COG3170    71 RVTSSRPVNEP--FLDFLVEVNWPSGRLVREYTL-LLDPPAYAAAAAAPAAAPAPAPAAPAAAAAAADQPAAEAA--PAA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2221 AHPPGTPRPGISVPysqPPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPAlpgplvrppdtcSQTPRPPGPgl 2300
Cdd:COG3170   146 SGEYYPVRPGDTLW---SIAARPVRPSSGVSLDQMMVALYRANPDAFIDGNINRLKA------------GAVLRVPAA-- 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2301 sDTFSRVSPSAARDPYdqspmtpRSQSDSFGTSQTAHDVADQPRPGSEgsfcASSNSPMHSQGQQFSGVSQLPGPVPTSG 2380
Cdd:COG3170   209 -EEVAALSPAEARQEV-------QAQSADWAAYRARLAAAVEPAPAAA----APAAPPAAAAAAGPVPAAAEDTLSPEVT 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2381 VTDTQNTVNMAQADTEKLRQR-QKLREIILQQQQQKKIAGRQEKGSQDSPAV-PHPGPLQHWQPENVNQAFTRPPPPYPG 2458
Cdd:COG3170   277 AAAAAEEADALPEAAAELAERlAALEAQLAELQRLLALKNPAPAAAVSAPAAaAAAATVEAAAPAAAAQPAAAAPAPALD 356

                         330
                  ....*....|...
gi 578814480 2459 NirsPVAPPLGPR 2471
Cdd:COG3170   357 N---PLLLAGLLR 366

PHA03378

EBNA-3B; Provisional

2237-2637

2.77e-04

EBNA-3B; Provisional

Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 47.37 E-value: 2.77e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2237 QPPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRP---PDTCSQTPRPPGPGL-------SDTFSR 2306
Cdd:PHA03378  440 QPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQAPLEPWQPLPHPQVTPvilHQPPAQGVQAHGSMLdllekddEDMEQR 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2307 VSpSAARDPYDQSPMTPRS-----------QSDSFGTSQTAHDvADQPRPGSEGSFCASSNSPMHSQGQQFS-GVSQLPG 2374
Cdd:PHA03378  520 VM-ATLLPPSPPQPRAGRRapcvytedldiESDEPASTEPVHD-QLLPAPGLGPLQIQPLTSPTTSQLASSApSYAQTPW 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2375 PVPTSGVTDTQNTVNMAQADTEKLRQ-RQKLREIILQQQQQKKIAGRQEKG-SQDSPAVPHPGPLQH---------WQPE 2443
Cdd:PHA03378  598 PVPHPSQTPEPPTTQSHIPETSAPRQwPMPLRPIPMRPLRMQPITFNVLVFpTPHQPPQVEITPYKPtwtqighipYQPS 677

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2444 NVNQAFT----------RPPPPYPGNIRSPVAPPLGPRYavfPKDQRGPYPPDVASMG-MRPhgfrfgfPGGSHGTMPSQ 2512
Cdd:PHA03378  678 PTGANTMlpiqwapgtmQPPPRAPTPMRPPAAPPGRAQR---PAAATGRARPPAAAPGrARP-------PAAAPGRARPP 747

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2513 ERF---LVPPQQIQGSGVSPQLRRSVSVDMPRP-LNNSQMNNPVGLPQHF-SPQSLPVQQHNILGQAYIELRHRAPDGRQ 2587
Cdd:PHA03378  748 AAApgrARPPAAAPGRARPPAAAPGAPTPQPPPqAPPAPQQRPRGAPTPQpPPQAGPTSMQLMPRAAPGQQGPTKQILRQ 827

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480 2588 RLPFSAPPG--SVVEASSNLRHGNFIPRPDfPGPRHTD-----PMRRPPQGLPNQLP 2637
Cdd:PHA03378  828 LLTGGVKRGrpSLKKPAALERQAAAGPTPS-PGSGTSDkivqaPVFYPPVLQPIQVM 883

COG5141

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

4444-4558

6.46e-04

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

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 46.13 E-value: 6.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4444 PKDYRKCCFCHEEgDGLtdgparLLNLDLDLWVHLNCALWSTEVY--ETQAGALINVELALRRGL-QMKCVFCHKTGATS 4520
Cdd:COG5141   244 EYQIRCCSFCPSS-DGA------FKQTSDGRWGHVICAMFNPELSfgHLLSKDPIDNIASVSSSRwKLGCLICKEFGGTC 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 4521 -GCHRFRCTNIYHFTCAIKAqCMFFK------------DKTMLCPMHKPKG 4558
Cdd:COG5141   317 iQCSYFNCTRAYHVTCARRA-GYFDLniyshngisyciDHEPLCRKHYPLG 366

PHD

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

1088-1137

1.03e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 39.89 E-value: 1.03e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 578814480   1088 CPVCYRNYREEDLIlQCRQCDRWMHAVCQNLNTEEEVENVadiGFDCSMC 1137
Cdd:smart00249    2 CSVCGKPDDGGELL-QCDGCDRWYHQTCLGPPLLEEEPDG---KWYCPKC 47

PHD

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

4510-4554

1.82e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 39.12 E-value: 1.82e-03

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578814480   4510 CVFCHKTGATS---GCHRfrCTNIYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:smart00249    2 CSVCGKPDDGGellQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

mukB

PRK04863

chromosome partition protein MukB;

3195-3288

2.47e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.47e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 3195 KQYEEWLQETQQLLQMQQKY--LEEQIGAHRKSKKALsakQRTAKKAGREFPEEDA---------EQLKHVTEQQSMVQK 3263
Cdd:PRK04863  503 RRLREQRHLAEQLQQLRMRLseLEQRLRQQQRAERLL---AEFCKRLGKNLDDEDEleqlqeeleARLESLSESVSEARE 579

                          90       100
                  ....*....|....*....|....*
gi 578814480 3264 QLEQIRKQQKEHAELIEDYRIKQQQ 3288
Cdd:PRK04863  580 RRMALRQQLEQLQARIQRLAARAPA 604

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

3189-3295

5.22e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 3189 VNDSQRKQYEEwLQETQQLLQMQQKYLEEQigahRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQI 3268
Cdd:COG4942   144 LAPARREQAEE-LRADLAELAALRAELEAE----RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                          90       100
                  ....*....|....*....|....*..
gi 578814480 3269 RKQQKEHAELIEDYRIKQQQQCAMAPP 3295
Cdd:COG4942   219 QQEAEELEALIARLEAEAAAAAERTPA 245

Name

Accession

Description

Interval

E-value

SET_KMT2C_2D

cd19171

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

4806-4958

1.75e-117

Pssm-ID: 380948 [Multi-domain] Cd Length: 153 Bit Score: 368.68 E-value: 1.75e-117

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4806 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 4885
Cdd:cd19171     1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4886 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4958
Cdd:cd19171    81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153

SET_KMT2C

cd19208

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

4805-4958

3.58e-108

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: 342.38 E-value: 3.58e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4805 SKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVID 4884
Cdd:cd19208     1 SKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578814480 4885 ATLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4958
Cdd:cd19208    81 ATLTGGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 154

SET_KMT2D

cd19209

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

4804-4958

2.02e-94

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: 302.77 E-value: 2.02e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4804 HSKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVI 4883
Cdd:cd19209     1 HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578814480 4884 DATLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4958
Cdd:cd19209    81 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155

ePHD2_KMT2C

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

4450-4554

4.95e-74

Pssm-ID: 277167 Cd Length: 105 Bit Score: 242.26 E-value: 4.95e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15697     1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                          90       100
                  ....*....|....*....|....*
gi 578814480 4530 IYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:cd15697    81 VYHFTCAIKAQCMFFKDKTMLCPMH 105

SET_SETD1-like

cd10518

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

4807-4955

7.82e-73

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: 240.96 E-value: 7.82e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4807 SSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQN-RGVYMFRMDNDHVIDA 4885
Cdd:cd10518     2 SKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVIDA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4886 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNCR 4955
Cdd:cd10518    82 TKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEE-KIPCLCGAPNCR 150

ePHD2_KMT2C_like

cd15666

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

4450-4554

2.26e-70

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: 231.81 E-value: 2.26e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15666     1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                          90       100
                  ....*....|....*....|....*
gi 578814480 4530 IYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:cd15666    81 VYHLPCAIKDGCMFFKDKTMLCPSH 105

ePHD2_KMT2D

cd15698

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

4450-4555

9.45e-66

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: 218.77 E-value: 9.45e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15698     1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                          90       100
                  ....*....|....*....|....*.
gi 578814480 4530 IYHFTCAIKAQCMFFKDKTMLCPMHK 4555
Cdd:cd15698    81 VYHFACAIRAKCMFFKDKTMLCPMHK 106

SET_KMT2A_2B

cd19170

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

4807-4959

3.41e-60

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: 204.93 E-value: 3.41e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4807 SSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDAT 4886
Cdd:cd19170     2 AMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDAT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4887 LTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWMN 4959
Cdd:cd19170    82 MHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDV--KIPCTCGSKKCRKYLN 152

ePHD1_KMT2C

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

248-331

3.33e-55

Pssm-ID: 277166 Cd Length: 90 Bit Score: 187.84 E-value: 3.33e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  248 GTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLL 327
Cdd:cd15696     7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86


                  ....
gi 578814480  328 CPEH 331
Cdd:cd15696    87 CPTH 90

HMG-box_KMT2C

cd22026

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...

1650-1730

2.63e-54

Pssm-ID: 438835 Cd Length: 81 Bit Score: 184.99 E-value: 2.63e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1650 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 1729
Cdd:cd22026     1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80


                  .
gi 578814480 1730 N 1730
Cdd:cd22026    81 N 81

SET_SETD1

cd19169

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

4818-4955

2.95e-54

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: 187.54 E-value: 2.95e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRG-VYMFRMDNDHVIDATLTGGPARYIN 4896
Cdd:cd19169    12 KKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGsSYLFRVDDDTIIDATKCGNLARFIN 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4897 HSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCR 4955
Cdd:cd19169    92 HSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDE--KIPCLCGAPQCR 148

SET_SET1

cd20072

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

4818-4955

8.01e-49

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: 172.22 E-value: 8.01e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRG-VYMFRMDNDHVIDATLTGGPARYIN 4896
Cdd:cd20072    12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDATKKGNIARFIN 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4897 HSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCR 4955
Cdd:cd20072    92 HCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREED--KIPCLCGAPNCR 148

SET_KMT2A

cd19206

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

4809-4959

4.57e-47

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: 167.51 E-value: 4.57e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4809 QYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLT 4888
Cdd:cd19206     4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578814480 4889 GGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN 4959
Cdd:cd19206    84 GNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154

SET_KMT2B

cd19207

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

4809-4959

4.05e-44

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: 159.03 E-value: 4.05e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4809 QYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLT 4888
Cdd:cd19207     4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578814480 4889 GGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN 4959
Cdd:cd19207    84 GNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 154

ePHD1_KMT2C_like

cd15665

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

248-331

6.61e-43

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: 152.86 E-value: 6.61e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  248 GTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLL 327
Cdd:cd15665     7 GEVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGCFQDIKTLTLF 86


                  ....
gi 578814480  328 CPEH 331
Cdd:cd15665    87 CPEH 90

HMG_KMT2C-like

cd21997

high mobility group (HMG)-box found in histone-lysine N-methyltransferases KMT2C, KMT2D and ...

1655-1721

1.04e-41

high mobility group (HMG)-box found in histone-lysine N-methyltransferases KMT2C, KMT2D and similar proteins; This subfamily includes KMT2C and KMT2D. KMT2C, also called myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) 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, and 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 called 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. All subfamily members contain one HMG-box domain.

Pssm-ID: 438813 Cd Length: 67 Bit Score: 148.66 E-value: 1.04e-41

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480 1655 KWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAAL 1721
Cdd:cd21997     1 KWEKDEPLGDMATISPVLYANINHPNLKQEYPDWTDRAKQIAKLWRKLSAEERAPYLQKARENRAAL 67

HMG-box_KMT2D

cd22027

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and ...

1646-1727

7.03e-40

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D, also called 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.

Pssm-ID: 438836 Cd Length: 84 Bit Score: 144.07 E-value: 7.03e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1646 MSNAQRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINK 1725
Cdd:cd22027     2 LSYNQRSLQRWEKDEELGELSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINK 81


                  ..
gi 578814480 1726 VQ 1727
Cdd:cd22027    82 VQ 83

SET_SETD1A

cd19204

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

4818-4959

1.22e-39

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: 145.94 E-value: 1.22e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGV-YMFRMDNDHVIDATLTGGPARYIN 4896
Cdd:cd19204    13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLARFIN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4897 HSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWMN 4959
Cdd:cd19204    93 HCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIEDN--KIPCLCGTENCRGTLN 153

SET

COG2940

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

4818-4957

2.01e-38

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 141.64 E-value: 2.01e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgvYMFRMDNDHVIDATLTGGPARYINH 4897
Cdd:COG2940     5 HPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4898 SCAPNCVAEvvtfERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHkiPCHCGavNCRKW 4957
Cdd:COG2940    83 SCDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134

SET_SETD1B

cd19205

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

4818-4959

1.20e-37

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: 140.19 E-value: 1.20e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGV-YMFRMDNDHVIDATLTGGPARYIN 4896
Cdd:cd19205    13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDATKCGNFARFIN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4897 HSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDqhKIPCHCGAVNCRKWMN 4959
Cdd:cd19205    93 HSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDV--KIPCLCGSENCRGTLN 153

ePHD_KMT2A_like

cd15664

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

4450-4554

2.82e-37

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: 137.15 E-value: 2.82e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15664     1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                          90       100
                  ....*....|....*....|....*
gi 578814480 4530 IYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:cd15664    81 NYHFMCARKAECVFQDDKKVFCPAH 105

PHD4_KMT2C

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

953-1009

8.51e-37

Pssm-ID: 277071 Cd Length: 57 Bit Score: 134.37 E-value: 8.51e-37

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480  953 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 1009
Cdd:cd15596     1 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 57

SET

smart00317

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

4820-4941

1.05e-35

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: 133.61 E-value: 1.05e-35

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   4820 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNR-GVYMFRMDNDHVIDATLTGGPARYINHS 4898
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHS 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 578814480   4899 CAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDD 4941
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

ePHD_KMT2A

cd15693

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...

4448-4555

7.63e-34

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: 127.81 E-value: 7.63e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4448 RKCCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRC 4527
Cdd:cd15693     1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                          90       100
                  ....*....|....*....|....*...
gi 578814480 4528 TNIYHFTCAIKAQCMFFKDKTMLCPMHK 4555
Cdd:cd15693    81 TSNYHFMCSRAKNCVFLEDKKVYCQRHK 108

PHD6_KMT2C

cd15600

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1087-1137

2.12e-32

Pssm-ID: 277073 Cd Length: 51 Bit Score: 121.58 E-value: 2.12e-32

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1087 SCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVADIGFDCSMC 1137
Cdd:cd15600     1 TCPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC 51

SET_SETD2

cd19172

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

4819-4958

3.11e-32

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: 124.23 E-value: 3.11e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4819 SNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRM-DNDHVIDATLTGGPARYINH 4897
Cdd:cd19172     2 AKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFMAlKSDEIIDATKKGNLSRFINH 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4898 SCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFD--FEDDQhkiPCHCGAVNCRKWM 4958
Cdd:cd19172    82 SCEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFEryGKEAQ---KCYCGSPNCRGYI 141

SET_SETD2-like

cd10531

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

4820-4955

4.30e-32

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: 123.52 E-value: 4.30e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4820 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQN-RGVYMFRMDNDHVIDATLTGGPARYINHS 4898
Cdd:cd10531     1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGkSNFYILSLSDDVVIDATRKGNLSRFINHS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578814480 4899 CAPNCVAEvVTFERGHKII-ISSSRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNCR 4955
Cdd:cd10531    81 CEPNCETQ-KWIVNGEYRIgIFALRDIPAGEELTFDYNFVNYNEA-KQVCLCGAQNCR 136

SET_ASHR3-like

cd19175

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

4830-4958

1.83e-31

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: 122.14 E-value: 1.83e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTIIRNEVAnrKEKLYESQNRG---VYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAE 4906
Cdd:cd19175    11 GWGLVADEDINAGEFIIEYVGEVIDDKTC--EERLWDMKHKGeknFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQ 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4907 VVTFERGHKIIISSSRRIQKGEELCYDYKF-DFEDDQHkipCHCGAVNCRKWM 4958
Cdd:cd19175    89 KWQVDGETRIGVFAIRDIKKGEELTYDYQFvQFGADQD---CHCGSKNCRGKL 138

SET_NSD

cd19173

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

4830-4954

2.05e-31

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, NSD2, NSD3 and similar proteins; The nuclear receptor-binding SET Domain (NSD) family of histone H3 lysine 36 methyltransferases is comprised of NSD1, NSD2, and NSD3, which are primarily known to be involved in chromatin integrity and gene expression through mono-, di-, or tri-methylating lysine 36 of histone H3 (H3K36), respectively. NSD1 (EC 2.1.1.43; also termed histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B) or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3.

Pssm-ID: 380950 [Multi-domain] Cd Length: 142 Bit Score: 122.04 E-value: 2.05e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAEVV 4908
Cdd:cd19173    13 GWGLRTKRDIKKGDFVIEYVGELIdEEECRRRLKKAHENNITNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQPNCETQKW 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 4909 TFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNC 4954
Cdd:cd19173    93 TVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNE-KKVCRCGAPNC 137

SET_EZH

cd10519

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

4821-4934

6.42e-31

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

Pssm-ID: 380917 Cd Length: 117 Bit Score: 119.66 E-value: 6.42e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4821 VYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGvYMFRMDNDHVIDATLTGGPARYINHSCA 4900
Cdd:cd10519     3 LLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSN 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578814480 4901 PNCVAEVVTFERGHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd10519    82 PNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDY 115

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

1010-1056

1.95e-30

Pssm-ID: 276988 Cd Length: 47 Bit Score: 115.65 E-value: 1.95e-30

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1056
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

PHD4_KMT2C_like

cd15512

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD domain 3 found in ...

960-1008

1.53e-29

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

Pssm-ID: 276987 Cd Length: 49 Bit Score: 113.33 E-value: 1.53e-29

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  960 MCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLEC 1008
Cdd:cd15512     1 MCVSCGSFGRGAEGRLIACSQCGQCYHPYCVNVKVTKVILSKGWRCLDC 49

SET

pfam00856

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

4830-4935

1.99e-29

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 115.31 E-value: 1.99e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  4830 GLGLYAARDIEKHTMVIEYIGT-IIRNEVANRKEKLYESQNR----GVYMFRMDND--HVIDATLT--GGPARYINHSCA 4900
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDEDseYCIDARALyyGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 578814480  4901 PNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYK 4935
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

ePHD1_KMT2D

cd15695

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

248-331

2.49e-29

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: 114.24 E-value: 2.49e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  248 GTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLL 327
Cdd:cd15695     7 GECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGSFQSMKTLLLL 86


                  ....
gi 578814480  328 CPEH 331
Cdd:cd15695    87 CPEH 90

SET_SUV39H

cd10542

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

4830-4958

4.22e-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: 118.94 E-value: 4.22e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgVYMFRMD-----NDHVIDATLTGGPARYINHSCAPN-- 4902
Cdd:cd10542    99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDyndddCEYTVDAAYYGNISHFINHSCDPNla 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4903 ---CVAEVVtFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQH----------KIPCHCGAVNCRKWM 4958
Cdd:cd10542   178 vyaVWINHL-DPRLPRIAFFAKRDIKAGEELTFDYLMTGTGGSSestipkpkdvRVPCLCGSKNCRKYL 245

PHD2_KMT2C

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

391-436

5.40e-29

Pssm-ID: 277069 Cd Length: 46 Bit Score: 111.57 E-value: 5.40e-29

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15594     1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

ePHD

cd15571

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...

4450-4554

6.56e-29

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: 113.83 E-value: 6.56e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPArLLNLDLDLWVHLNCALWSTEVYETQAGAL--INVELALRRGLQMKCVFCHKT-GATSGCHRFR 4526
Cdd:cd15571     1 CALCPRSGGALKGGGA-LKTTSDGLWVHVVCALWSPEVYFDDGTLLevEGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 578814480 4527 CTNIYHFTCAIKAQCMF-----FKDKTMLCPMH 4554
Cdd:cd15571    80 CPRSFHVSCAIRAGCLFefedgPGNFVVYCPKH 112

PHD3_KMT2C

cd15511

PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

467-518

8.50e-28

Pssm-ID: 276986 Cd Length: 52 Bit Score: 108.34 E-value: 8.50e-28

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  467 LCPFCGKCYHPELQKDMLHCNMCKRWVHLECDKPTDHELDTQLKEEYICMYC 518
Cdd:cd15511     1 PCPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52

PHD3_KMT2D

cd15597

PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

959-1008

4.54e-27

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

Pssm-ID: 277072 Cd Length: 51 Bit Score: 106.27 E-value: 4.54e-27

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480  959 DMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLEC 1008
Cdd:cd15597     1 DMCVVCGSFGRGSEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 50

ePHD_KMT2B

cd15694

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...

4450-4554

5.61e-27

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: 107.82 E-value: 5.61e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15694     1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                          90       100
                  ....*....|....*....|....*
gi 578814480 4530 IYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:cd15694    81 NFHFMCARASRCCFQDDKKVFCQKH 105

SET_ASH1L

cd19174

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

4830-4959

1.58e-26

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: 108.15 E-value: 1.58e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYeSQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCvaEVV 4908
Cdd:cd19174    11 GWGVRTKEPIKAGQFIIEYVGEVVsEQEFRRRMIEQY-HNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSCDPNC--EMQ 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4909 TFE-RG-HKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN 4959
Cdd:cd19174    88 KWSvNGvYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG 140

PHD6_KMT2C_like

cd15514

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in ...

1087-1137

1.03e-25

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

Pssm-ID: 276989 Cd Length: 51 Bit Score: 102.36 E-value: 1.03e-25

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1087 SCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVADIGFDCSMC 1137
Cdd:cd15514     1 KCPVCSRSYNEGELIIQCSQCERWLHGACDSLRTEEEAERAADNGYRCLLC 51

PHD2_KMT2C_like

cd15510

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

391-436

1.85e-25

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (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 plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions. This model corresponds to the second PHD finger.

Pssm-ID: 276985 Cd Length: 46 Bit Score: 101.36 E-value: 1.85e-25

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15510     1 VCQACRQPGDDTKMLVCETCDKGYHTSCLRPVMSSIPKYGWKCKNC 46

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

4658-4745

2.60e-24

Pssm-ID: 197781 Cd Length: 86 Bit Score: 99.68 E-value: 2.60e-24

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   4658 VFVIRIVEQGheDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENYTF 4737
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78


                    ....*...
gi 578814480   4738 RYGRNPLM 4745
Cdd:smart00542   79 RYHRSPLL 86

PHA03247

large tegument protein UL36; Provisional

1893-2370

5.64e-24

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 112.72 E-value: 5.64e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1893 PPSPQVFSPGSSNSRPPSPMdpYAkmvgtPRPP-PVGHSFSRRNSAAPvENCTPLSSVSRPLQMNETTANRPSPvrdlcs 1971
Cdd:PHA03247 2553 PPLPPAAPPAAPDRSVPPPR--PA-----PRPSePAVTSRARRPDAPP-QSARPRAPVDDRGDPRGPAPPSPLP------ 2618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1972 ssttnndPYAKPPDTPRPvmtdqfpkslglSRSPVVSEQTAKGPIAAGTSDHFTK-PSPRAdvFQRQRIPDSYARPlltp 2050
Cdd:PHA03247 2619 -------PDTHAPDPPPP------------SPSPAANEPDPHPPPTVPPPERPRDdPAPGR--VSRPRRARRLGRA---- 2673

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2051 apldsgPGPFKTPMQP-PPSSQDPYGSVSQASRRLSVDPYERPA------LTPRPIDNFSHNQSNDPYSQPPLTPHPAVN 2123
Cdd:PHA03247 2674 ------AQASSPPQRPrRRAARPTVGSLTSLADPPPPPPTPEPAphalvsATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2124 ESFAHPSRAFSQPGTISRPTSQDPYSQPPGTP-----RPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQTP 2198
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP 2827

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2199 RPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPGISV----PYSQPPATP----RPRIsegftrSSMTRPVLMPNQDPFLQA 2270
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVrrrpPSRSPAAKPaapaRPPV------RRLARPAVSRSTESFALP 2901

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2271 A-------QNRGPALPGPLVRPPDTCSQTPRPPGPGLSDT--FSRVSPSAARDPYDQSPmTPRSQSDSFGTSQTAHDVAD 2341
Cdd:PHA03247 2902 PdqperppQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPplAPTTDPAGAGEPSGAVP-QPWLGALVPGRVAVPRFRVP 2980

                         490       500
                  ....*....|....*....|....*....
gi 578814480 2342 QPRPGSEGSfcASSNSPMHsqGQQFSGVS 2370
Cdd:PHA03247 2981 QPAPSREAP--ASSTPPLT--GHSLSRVS 3005

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

344-389

8.99e-24

Pssm-ID: 276984 Cd Length: 48 Bit Score: 96.61 E-value: 8.99e-24

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480  344 NCAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAV--TPLKRAGWQCPEC 389
Cdd:cd15509     1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48

FYRC

pfam05965

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

4656-4740

1.11e-23

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

Pssm-ID: 461788 Cd Length: 83 Bit Score: 97.68 E-value: 1.11e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  4656 RPVFVIRIVEqgHEDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENY 4735
Cdd:pfam05965    1 GPLFRVTVEE--DPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78


                   ....*
gi 578814480  4736 TFRYG 4740
Cdd:pfam05965   79 KFRYG 83

SET_EZH2

cd19218

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

4817-4936

1.57e-23

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

Pssm-ID: 380995 Cd Length: 120 Bit Score: 98.83 E-value: 1.57e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4817 WKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYEsQNRGVYMFRMDNDHVIDATLTGGPARYIN 4896
Cdd:cd19218     2 SKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFAN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 578814480 4897 HSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKF 4936
Cdd:cd19218    81 HSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120

PHD2_KMT2D

cd15595

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

391-436

3.69e-23

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such asHOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the second PHD finger.

Pssm-ID: 277070 Cd Length: 46 Bit Score: 95.06 E-value: 3.69e-23

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15595     1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46

PHD5_KMT2D

cd15601

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1087-1137

6.75e-23

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such asHOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is downregulated in cholestasis. KMT2D contains the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the fifth PHD finger.

Pssm-ID: 277074 Cd Length: 51 Bit Score: 94.20 E-value: 6.75e-23

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1087 SCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVADIGFDCSMC 1137
Cdd:cd15601     1 TCPVCRAKYVEEDLLIQCRHCDRWVHAVCESLFTEDEVEQAADEGFDCSSC 51

SET_EZH1

cd19217

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

4818-4940

5.09e-22

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: 95.13 E-value: 5.09e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYEsQNRGVYMFRMDNDHVIDATLTGGPARYINH 4897
Cdd:cd19217     5 KKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANH 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578814480 4898 SCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFED 4940
Cdd:cd19217    84 SVNPNCYAKVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQAD 126

SET_SETDB-like

cd10538

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

4825-4934

5.56e-21

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: 94.75 E-value: 5.56e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4825 RSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYeSQNRGVYMFRMDND---------HVIDATLTGGPARYI 4895
Cdd:cd10538    95 RTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIY-DKSGGSYLFDLDEFsdsdgdgeeLCVDATFCGNVSRFI 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578814480 4896 NHSCAPN----CVAEVVTFERGHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd10538   174 NHSCDPNlfpfNVVIDHDDLRYPRIALFATRDILPGEELTFDY 216

SET_NSD2

cd19211

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

4823-4954

4.12e-20

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: 89.66 E-value: 4.12e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4823 LARSRIQGLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAP 4901
Cdd:cd19211     6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIdEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4902 NCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIpCHCGAVNC 4954
Cdd:cd19211    86 NCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTV-CRCGAPNC 137

ePHD_RAI1_like

cd15668

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...

4450-4554

4.29e-20

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: 88.13 E-value: 4.29e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFC--HEEGDGLTD--GPArllnldLDLWVHLNCALWSTEVYETqAGALINVELALRRGLQMKCVFCHKTGATSGCHRF 4525
Cdd:cd15668     1 CVFCkrGPHYKGLGDlfGPY------YEVWVHEDCAVWAPGVYLV-GGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHK 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 578814480 4526 RCTNIYHFTCAIKAQCMFFKDK-TMLCPMH 4554
Cdd:cd15668    74 GCKAKYHYPCAVESGCQLDEENfSLLCPKH 103

PHA03247

large tegument protein UL36; Provisional

1878-2315

3.17e-19

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 97.32 E-value: 3.17e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1878 RIPIQDSLSQAQTSQP-PSPqvfsPGSSNSRPPSPM-DPYAKMVGTPRPPPVGHSFSRRNSAAPVENCTP--LSSVSRPL 1953
Cdd:PHA03247 2599 RAPVDDRGDPRGPAPPsPLP----PDTHAPDPPPPSpSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAA 2674

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1954 QMNETTAN-RPSPVRDLCSSSTTNNDPYAkPPDTPRPVMTdqfPKSLGLSRSPVvsEQTAKGPIAAGTSDHFTKPSPRAD 2032
Cdd:PHA03247 2675 QASSPPQRpRRRAARPTVGSLTSLADPPP-PPPTPEPAPH---ALVSATPLPPG--PAAARQASPALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2033 VFQRQriPDSYARPLLTPAPLDSGPgPFKTPMQPPPSSQDPYG---SVSQASRRLSVDPYERPALTPRPIDNFSHNQSND 2109
Cdd:PHA03247 2749 ATPGG--PARPARPPTTAGPPAPAP-PAAPAAGPPRRLTRPAVaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2110 PYSQPPLTPHPAVNESFAHPSRAFSQPG--------TISRPTSQDPYSQPPGTPRPVVDSYSQSSgTARSnTDPYSQPPG 2181
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvapggdVRRRPPSRSPAAKPAAPARPPVRRLARPA-VSRS-TESFALPPD 2903

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2182 TPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRHSDPYAHP-----------------------PG--------TPRPG 2230
Cdd:PHA03247 2904 QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPttdpagagepsgavpqpwlgalvPGrvavprfrVPQPA 2983

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2231 ISVPYSQPPATPR-----PRISE-----GFTRSSMTRPV-----LMPNQDP--------FLQAAQNRGPALPGPLvrPPD 2287
Cdd:PHA03247 2984 PSREAPASSTPPLtghslSRVSSwasslALHEETDPPPVslkqtLWPPDDTedsdadslFDSDSERSDLEALDPL--PPE 3061

                         490       500
                  ....*....|....*....|....*...
gi 578814480 2288 TCSQTPRPPGPGLSDTFSRVSPSAARDP 2315
Cdd:PHA03247 3062 PHDPFAHEPDPATPEAGARESPSSQFGP 3089

SET_EHMT

cd10543

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

4818-4955

6.20e-19

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

Pssm-ID: 380941 [Multi-domain] Cd Length: 231 Bit Score: 89.32 E-value: 6.20e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4818 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyESqnrgvYMFRMDND----HVIDATLTGGPAR 4893
Cdd:cd10543    90 RYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRED--DS-----YLFDLDNKdgetYCIDARRYGNISR 162

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4894 YINHSCAPNCVAevVTFERGH------KIIISSSRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCR 4955
Cdd:cd10543   163 FINHLCEPNLIP--VRVFVEHqdlrfpRIAFFASRDIKAGEELGFDYGEKFWRIKGKyFTCRCGSPKCK 229

SET_SETD8

cd10528

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

4827-4934

9.32e-19

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: 85.71 E-value: 9.32e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4827 RIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYES-QNRGVYM--FRMDN-DHVIDATL-TGGPARYINHSC-A 4900
Cdd:cd10528    25 DGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYAKdPSTGCYMyyFQYKGkTYCVDATKeSGRLGRLINHSKkK 104

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578814480 4901 PNCVAEVVTFERGHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd10528   105 PNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138

ePHD

cd15571

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...

242-331

4.62e-18

Pssm-ID: 277046 [Multi-domain] Cd Length: 112 Bit Score: 82.63 E-value: 4.62e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  242 ALFDSTGTCWAHHRCVEWS--LGVCQMEEPLLVNVDKAVVSGSTERCAFCKH-LGATIKCCEEKCTQMYHYPCAAGAGTF 318
Cdd:cd15571    16 ALKTTSDGLWVHVVCALWSpeVYFDDGTLLEVEGVSKIPKRRKKLKCSICGKrGGACIQCSYPGCPRSFHVSCAIRAGCL 95

                          90
                  ....*....|....*..
gi 578814480  319 QDFS----HIFLLCPEH 331
Cdd:cd15571    96 FEFEdgpgNFVVYCPKH 112

FYRN

pfam05964

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

4599-4650

4.70e-18

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: 80.63 E-value: 4.70e-18

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  4599 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 4650
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

SET_NSD3

cd19212

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

4829-4954

1.06e-17

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: 82.67 E-value: 1.06e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4829 QGLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAEV 4907
Cdd:cd19212    12 RGWGLRTKRSIKKGEFVNEYVGELIdEEECRLRIKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQK 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 4908 VTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIpCHCGAVNC 4954
Cdd:cd19212    92 WTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTE-CHCGADNC 137

ePHD1_KMT2C_like

cd15665

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

4450-4554

3.10e-17

Pssm-ID: 277135 Cd Length: 90 Bit Score: 79.67 E-value: 3.10e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCheegdgltdgparllNLDlDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTN 4529
Cdd:cd15665     1 CALC---------------NLG-EVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSK 64

                          90       100
                  ....*....|....*....|....*..
gi 578814480 4530 IYHFTCAIKAQCmF--FKDKTMLCPMH 4554
Cdd:cd15665    65 SFHFPCAAAAGC-FqdIKTLTLFCPEH 90

SET_LegAS4-like

cd10522

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

4830-4940

1.17e-16

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: 78.92 E-value: 1.17e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNrgvYMFRMDNDH-VIDATLTGGPARYINHSCAPNCVAEVV 4908
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPL---YPFDLNGDIlVIDAGKKGNLTRFINHSDQPNLELIVR 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 578814480 4909 TFERGHKIIISSSRRIQKGEELCYDYKFDFED 4940
Cdd:cd10522    91 TLKGEQHIGFVAIRDIKPGEELFISYGPKYWK 122

PHA03247

large tegument protein UL36; Provisional

1907-2476

1.31e-16

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 88.46 E-value: 1.31e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1907 RPPSPMDPYAkmvGTPRPPPVGhsfsrrnSAAPVENCTPLSSVSRPLQMNETTANRPSPVRDLC-------SSSTTNNDP 1979
Cdd:PHA03247 2482 RPAEARFPFA---AGAAPDPGG-------GGPPDPDAPPAPSRLAPAILPDEPVGEPVHPRMLTwirgleeLASDDAGDP 2551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1980 YAKPPDTPRPVMTDQfpkslglsrsPVVSEQTAKGPIaagtsdhftKPSPRAdvfqRQRIPDSYARPLLTPAPLDSgPGP 2059
Cdd:PHA03247 2552 PPPLPPAAPPAAPDR----------SVPPPRPAPRPS---------EPAVTS----RARRPDAPPQSARPRAPVDD-RGD 2607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2060 FKTPMQPPPSSQDPYgsvsqasrrlSVDPyerPALTPRPIDNfshnqsNDPYSQPPLTPHPAVNESFAHPSRAfSQPGTI 2139
Cdd:PHA03247 2608 PRGPAPPSPLPPDTH----------APDP---PPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRV-SRPRRA 2667

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2140 SRPTSQDPYSQPPGTPRPvvDSYSQSSGTARSNTDPYSQPPgTPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRHSDP 2219
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRR--RAARPTVGSLTSLADPPPPPP-TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2220 YAHP--PGTPRPGISVPY-SQPPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPP 2296
Cdd:PHA03247 2745 PAGPatPGGPARPARPPTtAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2297 GPGLSDTFS--RVSPSAARDPYdQSPMTPRsqsdsfGTSQTAHDVADQPRPGSEGSFCASSNSPMhsqgqqfsgVSQLPG 2374
Cdd:PHA03247 2825 AGPLPPPTSaqPTAPPPPPGPP-PPSLPLG------GSVAPGGDVRRRPPSRSPAAKPAAPARPP---------VRRLAR 2888

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2375 PVPTsgvtdtQNTVNMAQADTEKLRQRQKlreiilqqqqqkkiagrqekgsqDSPAVPHPgplqhwQPENVNQAFTRPPP 2454
Cdd:PHA03247 2889 PAVS------RSTESFALPPDQPERPPQP-----------------------QAPPPPQP------QPQPPPPPQPQPPP 2933

                         570       580
                  ....*....|....*....|..
gi 578814480 2455 PYPGNIRSPVAPPLGPRYAVFP 2476
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEP 2955

SET_SUV39H_Clr4-like

cd20073

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

4829-4958

1.39e-16

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: 83.00 E-value: 1.39e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4829 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYEsqNRGV-YMFRMD-------NDHVIDATLTGGPARYINHSCA 4900
Cdd:cd20073   103 KGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYD--NVGVtYLFDLDlfedqvdEYYTVDAQYCGDVTRFINHSCD 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578814480 4901 PNCVAEVV----TFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQ----------------HKIPCHCGAVNCRKWM 4958
Cdd:cd20073   181 PNLAIYSVlrdkSDSKIYDLAFFAIKDIPALEELTFDYSGRNNFDQlgfignrsnskyinlkNKRPCYCGSANCRGWL 258

SET_SETMAR

cd10544

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

4830-4958

1.44e-16

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: 82.73 E-value: 1.44e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyeSQNRG----VYMFR--MDNDHV----IDATLTGGPARYINHSC 4899
Cdd:cd10544   101 GWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTK---SQTKGdmnyIIVLRehLSSGKVletfVDPTYIGNIGRFLNHSC 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578814480 4900 APNCVAEVVtfeRGH----KIIISSSRRIQKGEELCYDY------------KFDFEDDQHKIPCHCGAVNCRKWM 4958
Cdd:cd10544   178 EPNLFMVPV---RVDsmvpKLALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSRKPCLCGAENCRGFL 249

FYRN

smart00541

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...

4609-4652

1.47e-16

Pssm-ID: 128814 Cd Length: 44 Bit Score: 76.17 E-value: 1.47e-16

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 578814480   4609 LLPQQMQAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSIEE 4652
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44

SET_EHMT1

cd10535

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

4806-4955

2.46e-16

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: 81.52 E-value: 2.46e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4806 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRMDND----H 4881
Cdd:cd10535    78 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4882 VIDATLTGGPARYINHSCAPNCVAEVVTFE----RGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCR 4955
Cdd:cd10535   151 CIDARFYGNVSRFINHHCEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 229

SET_NSD1

cd19210

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

4819-4954

5.88e-16

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: 77.66 E-value: 5.88e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4819 SNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINH 4897
Cdd:cd19210     2 PEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIdEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480 4898 SCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNC 4954
Cdd:cd19210    82 CCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNG-KTVCKCGAPNC 137

ePHD_KMT2A_like

cd15664

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

250-331

8.13e-16

Pssm-ID: 277134 Cd Length: 105 Bit Score: 75.90 E-value: 8.13e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  250 CWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAG-TFQDFSHIFllC 328
Cdd:cd15664    25 EWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCARKAEcVFQDDKKVF--C 102


                  ...
gi 578814480  329 PEH 331
Cdd:cd15664   103 PAH 105

SET_SUV39H_DIM5-like

cd19473

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

4830-4958

1.16e-15

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

Pssm-ID: 380996 [Multi-domain] Cd Length: 274 Bit Score: 80.44 E-value: 1.16e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTIIRNEVAN-RKEKLYESQNRGVYMFRMD---NDHVIDATLTG-----------GPARY 4894
Cdd:cd19473   117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQrRRDAATIAQRKDVYLFALDkfsDPDSLDPRLRGdpyeidgefmsGPTRF 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4895 INHSCAPNC-VAEVVT------FergHKIIISSSRRIQKGEELCYDY----------KFDFEDDQHKIPCHCGAVNCRKW 4957
Cdd:cd19473   197 INHSCDPNLrIFARVGdhadkhI---HDLAFFAIKDIPRGTELTFDYvdgvtgldddAGDEEKEKEMTKCLCGSPKCRGY 273


                  .
gi 578814480 4958 M 4958
Cdd:cd19473   274 L 274

SET_EZH-like

cd19168

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

4821-4938

1.52e-15

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: 76.07 E-value: 1.52e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4821 VYLARSRIQ-GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgVYMFRMDNDHVIDATLTGGPARYINH-- 4897
Cdd:cd19168     3 VVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVSY-LYLFEEQEGIWVDAAIYGNLSRYINHat 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578814480 4898 --SCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDF 4938
Cdd:cd19168    82 dkVKTGNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNYGDNF 124

PHD1_Lid2p_like

cd15519

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

1010-1055

1.73e-15

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

Pssm-ID: 276994 [Multi-domain] Cd Length: 46 Bit Score: 73.27 E-value: 1.73e-15

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15519     1 GCEVCGLDDNEGEVLLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC 46

SET_SETD5-like

cd10529

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

4832-4938

1.73e-15

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: 75.77 E-value: 1.73e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4832 GLYAARDIEKHTMVIEYIGTI-IRNEVANRKEKLYESQNRgVYMF--RMDNDHVIDATLTGGPARYINHSCAPNCVAEVV 4908
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEVsLRSEFKEDNGFFKRPSPF-VFFYdgFEGLPLCVDARKYGNEARFIRRSCRPNAELRHV 96

                          90       100       110
                  ....*....|....*....|....*....|.
gi 578814480 4909 TFERG-HKIIISSSRRIQKGEELCYDYKFDF 4938
Cdd:cd10529    97 VVSNGeLRLFIFALKDIRKGTEITIPFDYDY 127

SET

cd08161

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

4820-4934

1.81e-15

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: 73.82 E-value: 1.81e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4820 NVYLARSRIQGLGLYAARDIEKhtmvieyiGTIIrnevanrkeklyesqnrgvymfrmdndhvidatltgGPARYINHSC 4899
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPK--------GEVI------------------------------------GLARFINHSC 36

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578814480 4900 APNCVAEVVTFERGHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd08161    37 EPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71

PHA03247

large tegument protein UL36; Provisional

2029-2613

2.20e-15

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 84.60 E-value: 2.20e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2029 PRADVFQRQriPDSYARPLLTPAPLDSGPGPFKTPMQPPPSSQDPyGSVSQASRRLSVDPyeRPALTPRPIDNFSHNQSN 2108
Cdd:PHA03247 2475 PGAPVYRRP--AEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAP-AILPDEPVGEPVHP--RMLTWIRGLEELASDDAG 2549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2109 DPYSQ-PPLTPHPAVNESFAHPSRAFSQPGTISRPTSQDPySQPPGTPRPvvdsysqssgtaRSNTDPYSQPPGTPRPTT 2187
Cdd:PHA03247 2550 DPPPPlPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRP-DAPPQSARP------------RAPVDDRGDPRGPAPPSP 2616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2188 VDPYSQQPQTPRPSTQtdlfvtpvtnqrhsdPYAHPPGTPRPGISVPYSQP---PATPRPRISEGFTRSSMTRPVLMPNQ 2264
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPS---------------PAANEPDPHPPPTVPPPERPrddPAPGRVSRPRRARRLGRAAQASSPPQ 2681

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2265 DPflqaaqnRGPALPGP------LVRPPDTCSQTPRPPGPGLSDTFSRVSPSAARDPYDQSPMTPRSQSDSFGTSQTAHD 2338
Cdd:PHA03247 2682 RP-------RRRAARPTvgsltsLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGP 2754

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2339 VADQPRPGSEGSfcASSNSPMhsqgqqfsgvsqlpGPVPTSGVTDTQNTVNMAQADTEKLRQRQKlreiiLQQQQQKKIA 2418
Cdd:PHA03247 2755 ARPARPPTTAGP--PAPAPPA--------------APAAGPPRRLTRPAVASLSESRESLPSPWD-----PADPPAAVLA 2813

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2419 GRQEKGSQDSPAVPHPGPlqhwqpenvNQAFTRPPPPYPGnirsPVAPPLGPRYAVFPK---DQRGP--YPPDVASMGMR 2493
Cdd:PHA03247 2814 PAAALPPAASPAGPLPPP---------TSAQPTAPPPPPG----PPPPSLPLGGSVAPGgdvRRRPPsrSPAAKPAAPAR 2880

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2494 PHGFRFGFPGGShgtmPSQERFLVPP--QQIQGSGVSPQLRRSVSVDMPRPLNNSQMNNPVGLPQHFSPQSLPVQQHNIL 2571
Cdd:PHA03247 2881 PPVRRLARPAVS----RSTESFALPPdqPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 2572 GQA-YIELRHRAPDG----RQRLPFSAPPGSVVEASSNLRHGNFIPR 2613
Cdd:PHA03247 2957 GAVpQPWLGALVPGRvavpRFRVPQPAPSREAPASSTPPLTGHSLSR 3003

SET_SUV39H2

cd10532

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

4829-4958

2.28e-15

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: 79.16 E-value: 2.28e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4829 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgVYMFRMD---NDHVIDATLTGGPARYINHSCAPNCVA 4905
Cdd:cd10532    95 RGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGI-TYLFDLDyesDEFTVDAARYGNVSHFVNHSCDPNLQV 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4906 EVVTFE----RGHKIIISSSRRIQKGEELCYDYKFDFEDD-------------QHKIPCHCGAVNCRKWM 4958
Cdd:cd10532   174 FNVFIDnldtRLPRIALFSTRTIKAGEELTFDYQMKGSGDlssdsidnspakkRVRTVCKCGAVTCRGYL 243

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

4477-4554

2.49e-15

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 73.90 E-value: 2.49e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  4477 HLNCALWSTEVYetQAGA------LINVELALRRGLQMKCVFCH-KTGATSGCHRFRCTNIYHFTCAIKAQCMF-FKDKT 4548
Cdd:pfam13771    1 HVVCALWSPELV--QRGNdsmgfpIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDN 78

                           90
                   ....*....|
gi 578814480  4549 ----MLCPMH 4554
Cdd:pfam13771   79 gtfkSYCKKH 88

SET_SUV39H1

cd10525

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

4829-4958

4.40e-15

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: 78.40 E-value: 4.40e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4829 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNrGVYMFRMD---NDHVIDATLTGGPARYINHSCAPNCVA 4905
Cdd:cd10525    97 RGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQV 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4906 EVVTF----ERGHKIIISSSRRIQKGEELCYDYKF-----DFEDDQH-----------------KIPCHCGAVNCRKWM 4958
Cdd:cd10525   176 YNVFIdnldERLPRIALFATRTIRAGEELTFDYNMqvdpvDAESTKMdsnfglaglpgspkkrvRIECKCGVRSCRKYL 254

PHD1_KDM5B

cd15603

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis ...

1010-1055

4.97e-15

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis antigen 31 (CT31), Histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A)) is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of pregnant females and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277076 Cd Length: 46 Bit Score: 71.91 E-value: 4.97e-15

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15603     1 VCLVCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC 46

PHD_BAZ1A

cd15627

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

392-436

5.47e-15

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

Pssm-ID: 277097 [Multi-domain] Cd Length: 46 Bit Score: 71.65 E-value: 5.47e-15

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15627     2 CRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC 46

PHD1_KDM5A_like

cd15515

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...

1010-1055

7.55e-15

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

Pssm-ID: 276990 Cd Length: 46 Bit Score: 71.27 E-value: 7.55e-15

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15515     1 ICQVCGRGDDEDKLLLCDGCDDSYHTFCLIPPLPDIPPGDWRCPKC 46

ePHD_TCF20

cd15699

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...

4450-4554

7.66e-15

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: 73.41 E-value: 7.66e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGD----GLTDGPArllnldLDLWVHLNCALWSTEVYETqAGALINVELALRRGLQMKCVFCHKTGATSGCHRF 4525
Cdd:cd15699     1 CCLCGKWANyrnlGDLFGPF------YEFWVHEGCILWANGIYLV-CGRLYGLQEALDIAREMKCSHCQEAGATLGCYNK 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 578814480 4526 RCTNIYHFTCAIKAQCMFFKDK-TMLCPMH 4554
Cdd:cd15699    74 GCSFRYHYPCAIDADCLLNEENfSVRCPKH 103

ePHD2_KMT2C_like

cd15666

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

251-331

1.20e-14

Pssm-ID: 277136 Cd Length: 105 Bit Score: 72.72 E-value: 1.20e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  251 WAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGT--FQDFShifLLC 328
Cdd:cd15666    26 WVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGCmfFKDKT---MLC 102


                  ...
gi 578814480  329 PEH 331
Cdd:cd15666   103 PSH 105

SET_EHMT2

cd10533

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

4806-4955

1.70e-14

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: 76.59 E-value: 1.70e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4806 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKlyesqnrGVYMFRMDND----H 4881
Cdd:cd10533    78 RNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4882 VIDATLTGGPARYINHSCAPNCVAEVVTFE----RGHKIIISSSRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCR 4955
Cdd:cd10533   151 CIDARYYGNISRFINHLCDPNIIPVRVFMLhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 229

PHD_RSF1

cd15543

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

1011-1055

5.15e-14

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

Pssm-ID: 277018 [Multi-domain] Cd Length: 46 Bit Score: 68.84 E-value: 5.15e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15543     2 CRKCGLSDHPEWILLCDRCDAGYHTACLRPPLMIIPDGNWFCPPC 46

PHD2_KMT2C

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1010-1055

8.25e-14

Pssm-ID: 277069 Cd Length: 46 Bit Score: 68.43 E-value: 8.25e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15594     1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

PHD1_Lid_like

cd15605

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...

1010-1055

1.19e-13

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

Pssm-ID: 277078 Cd Length: 46 Bit Score: 67.86 E-value: 1.19e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15605     1 VCHTCGRGDGEESMLLCDGCDDSYHTFCLLPPLSEVPKGDWRCPKC 46

PHA03307

transcriptional regulator ICP4; Provisional

2124-2536

1.39e-13

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 78.29 E-value: 1.39e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2124 ESFAHPSRAFSQPGTISRPTSQDPYSQPPG----TPRPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQTPR 2199
Cdd:PHA03307   12 EAAAEGGEFFPRPPATPGDAADDLLSGSQGqlvsDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2200 PSTQTdlfVTPVTNQRHSDPYAHPPGTPRPGISVPYSQPPATPRPRISE-----GFTRSSMTRPVLMPNQDPFLQAAQ-- 2272
Cdd:PHA03307   92 LSTLA---PASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgSPGPPPAASPPAAGASPAAVASDAas 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2273 NRGPALPGPLVRPPDTCSQTPRPPGPGLsdtfsrvSPSAARDPYDQSPMTPRSQSDSFGTSQTAHDVADQPRPGSegsfc 2352
Cdd:PHA03307  169 SRQAALPLSSPEETARAPSSPPAEPPPS-------TPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASS----- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2353 aSSNSPMHSQGQQFSGVSQLPGPVPTSGVTDTQntvnMAQADTEKLRQRQKLREiilqqqqqKKIAGRQEKGSQDSPAVP 2432
Cdd:PHA03307  237 -SDSSSSESSGCGWGPENECPLPRPAPITLPTR----IWEASGWNGPSSRPGPA--------SSSSSPRERSPSPSPSSP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2433 HPGP-------LQHWQPE-NVNQAFTRPPPPYPgnirSPVAPPLGPRYAVFPKDQRGPYPPDVASMGMRPHGFRFGFPGG 2504
Cdd:PHA03307  304 GSGPapsspraSSSSSSSrESSSSSTSSSSESS----RGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPA 379

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 578814480 2505 SHGTMPSQER--FLVPPQ--QIQGSGVSPQLRRSVS 2536
Cdd:PHA03307  380 ASAGRPTRRRarAAVAGRarRRDATGRFPAGRPRPS 415

PHD_BAZ1A

cd15627

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

1011-1055

1.78e-13

Pssm-ID: 277097 [Multi-domain] Cd Length: 46 Bit Score: 67.42 E-value: 1.78e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15627     2 CRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC 46

PHD2_KMT2C_like

cd15510

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

1010-1055

1.84e-13

Pssm-ID: 276985 Cd Length: 46 Bit Score: 67.46 E-value: 1.84e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15510     1 VCQACRQPGDDTKMLVCETCDKGYHTSCLRPVMSSIPKYGWKCKNC 46

ePHD2_KMT2C

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

251-331

1.89e-13

Pssm-ID: 277167 Cd Length: 105 Bit Score: 69.31 E-value: 1.89e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  251 WAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAG-TFqdFSHIFLLCP 329
Cdd:cd15697    26 WVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAIKAQcMF--FKDKTMLCP 103


                  ..
gi 578814480  330 EH 331
Cdd:cd15697   104 MH 105

PHD1_KDM5A

cd15602

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...

1010-1056

2.23e-13

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

Pssm-ID: 277075 Cd Length: 49 Bit Score: 67.28 E-value: 2.23e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1056
Cdd:cd15602     1 VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCV 47

ePHD_RAI1

cd15700

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...

4450-4554

2.23e-13

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

Pssm-ID: 277170 Cd Length: 104 Bit Score: 69.14 E-value: 2.23e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEegdgltdgPARLLNL-DL------DLWVHLNCALWSTEVYETqAGALINVELALRRGLQMKCVFCHKTGATSGC 4522
Cdd:cd15700     1 CCLCRN--------PANYKDLgDLcgpyypEHWVHEACAVWTTGVYLV-AGKLFGLQEAVQKAADAKCSSCQGAGATVGC 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 578814480 4523 HRFRCTNIYHFTCAIKAQCMFFKDK-TMLCPMH 4554
Cdd:cd15700    72 CHKGCTQSYHYICAVEAGCLFEEENfSLRCPKH 104

ePHD1_KMT2C

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

4473-4554

2.70e-13

Pssm-ID: 277166 Cd Length: 90 Bit Score: 68.43 E-value: 2.70e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4473 DLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCAIKAQCMF-FKDKTMLC 4551
Cdd:cd15696     8 ECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQdFSRRLLLC 87


                  ...
gi 578814480 4552 PMH 4554
Cdd:cd15696    88 PTH 90

PHD_BAZ2A_like

cd15545

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

392-436

3.10e-13

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

Pssm-ID: 277020 [Multi-domain] Cd Length: 46 Bit Score: 66.57 E-value: 3.10e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15545     2 CQICRSGDNEDQLLLCDGCDRGYHTYCFKPKMTNVPEGDWFCPEC 46

PHD_BAZ1A_like

cd15544

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

1011-1055

4.16e-13

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

Pssm-ID: 277019 Cd Length: 46 Bit Score: 66.28 E-value: 4.16e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15544     2 CKVCRKKGDPDNMILCDGCDKAFHLYCLRPALREVPSGDWFCPAC 46

SET_SETDB1

cd10517

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

4830-4956

4.89e-13

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: 73.09 E-value: 4.89e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLY--------------ESQNRGVYMFRMDNDHVIDATLTGGPARYI 4895
Cdd:cd10517   140 GWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYgdeyfaeldyievvEKLKEGYESDVEEHCYIIDAKSEGNLGRYL 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480 4896 NHSCAPNCVAEVVtFERGHKIIIS-----SSRRIQKGEELCYDYKFDFEDDQHKI-PCHCGAVNCRK 4956
Cdd:cd10517   220 NHSCSPNLFVQNV-FVDTHDLRFPwvaffASRYIRAGTELTWDYNYEVGSVPGKVlYCYCGSSNCRG 285

ePHD1_KMT2D

cd15695

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

4473-4554

6.48e-13

Pssm-ID: 277165 Cd Length: 90 Bit Score: 67.25 E-value: 6.48e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4473 DLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCAiKAQCMFFKDKT--ML 4550
Cdd:cd15695     8 ECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCA-AASGSFQSMKTllLL 86


                  ....
gi 578814480 4551 CPMH 4554
Cdd:cd15695    87 CPEH 90

ePHD_PHF6_like

cd15673

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...

4450-4554

6.57e-13

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: 68.19 E-value: 6.57e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGParLLNLDLDLWVHLNCALWSTEVYETQ-------AGALIN-VELALRRGLQMKCVFCHKTGATSG 4521
Cdd:cd15673     1 CGFCKSGEENKETGG--KLASGEKIAAHHNCMLFSSGLVQYVspnendfGGFDIEdVKKEIKRGRKLKCNLCKKTGATIG 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 578814480 4522 CHRFRCTNIYHFTCAIKAQCMFFKDK-----TMLCPMH 4554
Cdd:cd15673    79 CDVKQCKKTYHYHCAKKDDAKIIERNsqgiyRVYCKNH 116

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

391-436

7.38e-13

Pssm-ID: 276988 Cd Length: 47 Bit Score: 65.58 E-value: 7.38e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 46

PHD

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

1010-1056

1.01e-12

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 65.59 E-value: 1.01e-12

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 578814480  1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQT--VPKGGWKCKWCV 1056
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPaeIPSGEWLCPECK 49

ePHD_RAI1_like

cd15668

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...

251-331

1.08e-12

Pssm-ID: 277138 Cd Length: 103 Bit Score: 66.95 E-value: 1.08e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  251 WAHHRCVEWSLGVCqMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLLCPE 330
Cdd:cd15668    24 WVHEDCAVWAPGVY-LVGGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENFSLLCPK 102


                  .
gi 578814480  331 H 331
Cdd:cd15668   103 H 103

PHD1_KDM5C_5D

cd15604

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...

1010-1055

1.40e-12

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

Pssm-ID: 277077 Cd Length: 46 Bit Score: 64.86 E-value: 1.40e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15604     1 VCRMCSRGDEDDKLLLCDGCDDNYHTFCLLPPLPEPPKGIWRCPKC 46

PHD2_PHF10

cd15529

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

391-436

2.89e-12

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

Pssm-ID: 277004 Cd Length: 44 Bit Score: 63.86 E-value: 2.89e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQpvMKSVPTNGWKCKNC 436
Cdd:cd15529     1 TCTKCGDPHDEDKMMFCDQCDRGYHTFCVG--LRSIPDGRWICPLC 44

zf-HC5HC2H_2

pfam13832

PHD-zinc-finger like domain;

4448-4543

3.25e-12

PHD-zinc-finger like domain;

Pssm-ID: 463991 [Multi-domain] Cd Length: 109 Bit Score: 65.83 E-value: 3.25e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  4448 RKCCFCHEEGDGL---TDGparllnldldLWVHLNCALWSTEVY--ETQAGALINVELALRRGLQMKCVFCHK-TGATSG 4521
Cdd:pfam13832    1 VRCCLCPLRGGALkqtSDG----------RWVHVLCAIFVPEVRfgNVATMEPIDVSRIPPERWKLKCVFCKKrSGACIQ 70

                           90       100
                   ....*....|....*....|..
gi 578814480  4522 CHRFRCTNIYHFTCAIKAQCMF 4543
Cdd:pfam13832   71 CSKGRCTTAFHVTCAQAAGVYM 92

PHD_BAZ1A_like

cd15544

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

392-436

3.33e-12

Pssm-ID: 277019 Cd Length: 46 Bit Score: 63.97 E-value: 3.33e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15544     2 CKVCRKKGDPDNMILCDGCDKAFHLYCLRPALREVPSGDWFCPAC 46

ePHD_KMT2A

cd15693

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...

251-312

5.31e-12

Pssm-ID: 277163 Cd Length: 113 Bit Score: 65.41 E-value: 5.31e-12

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578814480  251 WAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 312
Cdd:cd15693    28 WTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCS 89

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

253-331

5.38e-12

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 64.66 E-value: 5.38e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   253 HHRCVEWSLGVCQ-----MEEPLLvNVDKAVVSGSTERCAFCKH-LGATIKCCEEKCTQMYHYPCAAGAG---TFQDFSH 323
Cdd:pfam13771    1 HVVCALWSPELVQrgndsMGFPIE-DIEKIPKRRWKLKCYLCKKkGGACIQCSKKNCRRAFHVTCALEAGllmQFDEDNG 79


                   ....*....
gi 578814480   324 IFLL-CPEH 331
Cdd:pfam13771   80 TFKSyCKKH 88

PHD_RSF1

cd15543

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

392-436

5.43e-12

Pssm-ID: 277018 [Multi-domain] Cd Length: 46 Bit Score: 63.06 E-value: 5.43e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15543     2 CRKCGLSDHPEWILLCDRCDAGYHTACLRPPLMIIPDGNWFCPPC 46

PHD_PHRF1

cd15536

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

1011-1055

5.52e-12

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

Pssm-ID: 277011 Cd Length: 46 Bit Score: 63.20 E-value: 5.52e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15536     2 CEVCGRSDREDRLLLCDGCDAGYHMECLTPPLDEVPIEEWFCPEC 46

PHD_UHRF1_2

cd15525

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...

1011-1055

6.37e-12

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

Pssm-ID: 277000 Cd Length: 47 Bit Score: 63.16 E-value: 6.37e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGG-WKCKWC 1055
Cdd:cd15525     2 CHVCGGKQDPEKQLLCDECDMAYHLYCLDPPLTSLPDDDeWYCPDC 47

ePHD_KMT2B

cd15694

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...

251-331

7.21e-12

Pssm-ID: 277164 Cd Length: 105 Bit Score: 65.06 E-value: 7.21e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  251 WAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA-AGAGTFQDFSHIFllCP 329
Cdd:cd15694    26 WTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCArASRCCFQDDKKVF--CQ 103


                  ..
gi 578814480  330 EH 331
Cdd:cd15694   104 KH 105

PHD_UHRF1

cd15616

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); ...

1011-1055

7.33e-12

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

Pssm-ID: 277088 Cd Length: 47 Bit Score: 63.06 E-value: 7.33e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVP-KGGWKCKWC 1055
Cdd:cd15616     2 CHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPdDEDWYCPEC 47

ePHD_PHF7_G2E3_like

cd15669

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...

4450-4554

1.02e-11

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: 64.58 E-value: 1.02e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGlTDGPARLLNLDlDLWVHLNCALWSTEVYETQ------AGALIN-VELALRRGLQMKCVFCHKTGATSGC 4522
Cdd:cd15669     1 CVLCGRSDDD-PDKYGEKLQKD-GICAHYFCLLFSSGLPQRGednegiYGFLPEdIRKEVRRASRLRCFYCKKKGASIGC 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578814480 4523 HRFRCTNIYHFTCAIKAQC--MFFKDKTMLCPMH 4554
Cdd:cd15669    79 AVKGCRRSFHFPCGLENGCvtQFFGEYRSFCWEH 112

PHD

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

1010-1055

1.38e-11

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 62.23 E-value: 1.38e-11

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578814480   1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQT-VPKGGWKCKWC 1055
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD2_KMT2D

cd15595

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1010-1055

1.49e-11

Pssm-ID: 277070 Cd Length: 46 Bit Score: 61.94 E-value: 1.49e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15595     1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46

ePHD_RAI1

cd15700

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...

251-331

1.85e-11

Pssm-ID: 277170 Cd Length: 104 Bit Score: 63.74 E-value: 1.85e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  251 WAHHRCVEWSLGVCQMEEPLLvNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLLCPE 330
Cdd:cd15700    25 WVHEACAVWTTGVYLVAGKLF-GLQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEENFSLRCPK 103


                  .
gi 578814480  331 H 331
Cdd:cd15700   104 H 104

SET_SETDB

cd10541

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

4829-4956

2.13e-11

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: 67.18 E-value: 2.13e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4829 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAEVV 4908
Cdd:cd10541   102 KGWGIRCLDDIAKGTFVCIYAGKILTDDFADKEGLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNV 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578814480 4909 tFERGHK-----IIISSSRRIQKGEELCYDYKFDFED-DQHKIPCHCGAVNCRK 4956
Cdd:cd10541   182 -FVDTHDlrfpwVAFFASKRIKAGTELTWDYNYEVGSvEGKELLCCCGSNECRG 234

PHD

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

391-439

3.12e-11

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 61.35 E-value: 3.12e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578814480   391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPV--MKSVPTNGWKCKNCRIC 439
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPldPAEIPSGEWLCPECKPK 51

SET_SMYD

cd20071

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

4830-4934

3.82e-11

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

Pssm-ID: 380997 [Multi-domain] Cd Length: 122 Bit Score: 63.17 E-value: 3.82e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4830 GLGLYAARDIEKhtmvieyiGTIIRNE------VANRKEKLYESQNRGVYMFRMdndhvidatltggpARYINHSCAPNC 4903
Cdd:cd20071    10 GRGLVATRDIEP--------GELILVEkplvsvPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA 67

                          90       100       110
                  ....*....|....*....|....*....|.
gi 578814480 4904 VaevVTFERGHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd20071    68 V---VVFDGNGTLRVRALRDIKAGEELTISY 95

PHD2_KAT6A_6B

cd15527

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

1008-1055

4.11e-11

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

Pssm-ID: 277002 Cd Length: 46 Bit Score: 60.85 E-value: 4.11e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480 1008 CTVCEACGKATDpgrLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15527     2 CSVCQDSGNADN---LLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46

PHD2_d4

cd15530

PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three ...

1011-1055

4.93e-11

PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes by changing the condensed/decondensed state of chromatin in the nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro-specific gene clusters. The d4 family proteins show distinct domain organization with domain 2/3 in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc finger in the central part and two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the second PHD finger.

Pssm-ID: 277005 Cd Length: 46 Bit Score: 60.48 E-value: 4.93e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15530     2 CSLCGTSENDDQLLFCDDCDRGYHMYCLSPPMSEPPEGSWSCHLC 46

PHD_BAZ2A_like

cd15545

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

1011-1055

5.39e-11

Pssm-ID: 277020 [Multi-domain] Cd Length: 46 Bit Score: 60.40 E-value: 5.39e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15545     2 CQICRSGDNEDQLLLCDGCDRGYHTYCFKPKMTNVPEGDWFCPEC 46

PHD1_KDM5A_like

cd15515

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...

391-436

6.32e-11

Pssm-ID: 276990 Cd Length: 46 Bit Score: 60.10 E-value: 6.32e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15515     1 ICQVCGRGDDEDKLLLCDGCDDSYHTFCLIPPLPDIPPGDWRCPKC 46

SET_SETDB2

cd10523

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

4829-4958

7.60e-11

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: 66.01 E-value: 7.60e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4829 QGLGLYAARDIEKHTMVIEYIGTI---IRNEVANRKEKLYESQNRGVYMFRM-----------DNDHVIDATLTGGPARY 4894
Cdd:cd10523   118 KGWGVRCLDDIDKGTFVCIYAGRVlsrARSPTEPLPPKLELPSENEVEVVTSwlilskkrklrENVCFLDASKEGNVGRF 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480 4895 INHSCAPNCVAEVVTFERGHK----IIISSSRRIQKGEELCYDYKFDFEDDQHK-IPCHCGAVNCRKWM 4958
Cdd:cd10523   198 LNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYSYDAGTSPEQeIPCLCGVNKCQKKI 266

SET_SpSET3-like

cd19183

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

4831-4945

9.20e-11

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: 63.96 E-value: 9.20e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4831 LGLYAARDIEKHTMVIEYIGtiirnEVANRKEKLYESQNRgvY----------MFRMDNDHVIDATLTGGPARYINHSCA 4900
Cdd:cd19183    14 FGLFADRPIPAGDPIQELLG-----EIGLQSEYIADPENQ--YqilgapkphvFFHPQSPLYIDTRRSGSVARFIRRSCR 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 4901 PNCVAEVVTFERGH--KIIISSSRRIQKGEELCYDYKFDFEDDQHKI 4945
Cdd:cd19183    87 PNAELVTVASDSGSvlKFVLYASRDISPGEEITIGWDWDNPHPFRRF 133

PHD1_KDM5C_5D

cd15604

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...

391-436

1.11e-10

Pssm-ID: 277077 Cd Length: 46 Bit Score: 59.47 E-value: 1.11e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15604     1 VCRMCSRGDEDDKLLLCDGCDDNYHTFCLLPPLPEPPKGIWRCPKC 46

ePHD_PHF7_G2E3_like

cd15669

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...

252-331

1.21e-10

Pssm-ID: 277139 [Multi-domain] Cd Length: 112 Bit Score: 61.50 E-value: 1.21e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  252 AHHRCVEWSLGVCQMEEP-------LLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGT-FQDFSH 323
Cdd:cd15669    25 AHYFCLLFSSGLPQRGEDnegiygfLPEDIRKEVRRASRLRCFYCKKKGASIGCAVKGCRRSFHFPCGLENGCvTQFFGE 104


                  ....*...
gi 578814480  324 IFLLCPEH 331
Cdd:cd15669   105 YRSFCWEH 112

ePHD2_KMT2D

cd15698

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

251-331

1.29e-10

Pssm-ID: 277168 Cd Length: 107 Bit Score: 61.22 E-value: 1.29e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  251 WAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGT--FQDFShifLLC 328
Cdd:cd15698    26 WVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIRAKCmfFKDKT---MLC 102


                  ...
gi 578814480  329 PEH 331
Cdd:cd15698   103 PMH 105

PHD_BAZ1B

cd15628

PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...

392-436

1.68e-10

PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also termed Tyrosine-protein kinase BAZ1B, or Williams syndrome transcription factor (WSTF), or Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, or WALp2, is a multifunctional protein implicated in several nuclear processes, including replication, transcription, and the DNA damage response. BAZ1B/WSTF, together with the imitation switch (ISWI) ATPase, forms a WSTF-ISWI chromatin remodeling complex (WICH), which transiently associates with the human inactive X chromosome (Xi) during late S-phase prior to BRCA1 and gamma-H2AX. Moreover, BAZ1B/WSTF, SNF2h, and nuclear myosin 1 (NM1) forms the chromatin remodeling complex B-WICH that is involved in regulating rDNA transcription. BAZ1B contains a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain.

Pssm-ID: 277098 Cd Length: 46 Bit Score: 58.99 E-value: 1.68e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15628     2 CKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC 46

PHD_UHRF2

cd15617

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...

1011-1055

1.75e-10

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

Pssm-ID: 277089 Cd Length: 47 Bit Score: 58.81 E-value: 1.75e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKG-GWKCKWC 1055
Cdd:cd15617     2 CYVCGGKQDAHMQLLCDECNMAYHIYCLNPPLDKIPEDeDWYCPSC 47

PHD_BAZ2A

cd15629

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

392-436

2.20e-10

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

Pssm-ID: 277099 Cd Length: 47 Bit Score: 58.71 E-value: 2.20e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15629     2 CLVCRKGDNDEYLLLCDGCDRGCHMYCHRPKMLQVPEGDWFCPNC 46

PHD2_CHD_II

cd15532

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

391-436

2.70e-10

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

Pssm-ID: 277007 [Multi-domain] Cd Length: 43 Bit Score: 58.45 E-value: 2.70e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEdskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15532     1 FCRVCKDGGE---LLCCDGCPSSYHLHCLNPPLAEIPDGDWFCPRC 43

Atrophin-1

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

2027-2382

2.72e-10

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 67.10 E-value: 2.72e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2027 PSPRADvfqrQRIPDSYARP--LLTPAPLDSGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDnfsh 2104
Cdd:pfam03154  149 PSPQDN----ESDSDSSAQQqiLQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQ---- 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2105 nqsndpySQPPLTPHPAVNESFA-HPSRAFS-----QPGTISRPTSQDPysqPPGTPRPVVDSYSQSSGTARSNTDPYSQ 2178
Cdd:pfam03154  221 -------TQSTAAPHTLIQQTPTlHPQRLPSphpplQPMTQPPPPSQVS---PQPLPQPSLHGQMPPMPHSLQTGPSHMQ 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2179 PPGTPRPTTVDPYSQQPQTP-RPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPG------ISVPYSQPP-ATPRPRISegf 2250
Cdd:pfam03154  291 HPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQplppapLSMPHIKPPpTTPIPQLP--- 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2251 TRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPGPGLSDTFSRVSPSAARDP-YDQSPMTPRSQSdS 2329
Cdd:pfam03154  368 NPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPvLTQSQSLPPPAA-S 446

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 578814480  2330 FGTSQTAHDVADQPrPGSEGSFCASSNSPMHS-QGQQFSGVSQLPGPVPTSGVT 2382
Cdd:pfam03154  447 HPPTSGLHQVPSQS-PFPQHPFVPGGPPPITPpSGPPTSTSSAMPGIQPPSSAS 499

PHD

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

391-436

2.88e-10

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 58.38 E-value: 2.88e-10

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578814480    391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKS-VPTNGWKCKNC 436
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD

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

961-1011

3.92e-10

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 58.27 E-value: 3.92e-10

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480   961 CVVCGsfGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKG-WRCLECTVC 1011
Cdd:pfam00628    2 CAVCG--KSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51

PHD1_Lid_like

cd15605

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...

391-436

4.42e-10

Pssm-ID: 277078 Cd Length: 46 Bit Score: 57.84 E-value: 4.42e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15605     1 VCHTCGRGDGEESMLLCDGCDDSYHTFCLLPPLSEVPKGDWRCPKC 46

PHD

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

960-1008

5.22e-10

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 57.61 E-value: 5.22e-10

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 578814480    960 MCVVCGSFGqgAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLEC 1008
Cdd:smart00249    1 YCSVCGKPD--DGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

PHD2_KAT6A_6B

cd15527

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

389-436

7.58e-10

Pssm-ID: 277002 Cd Length: 46 Bit Score: 57.00 E-value: 7.58e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480  389 CKVCQNckqSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15527     2 CSVCQD---SGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46

PHD2_CHD_II

cd15532

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

1010-1055

8.40e-10

Pssm-ID: 277007 [Multi-domain] Cd Length: 43 Bit Score: 56.91 E-value: 8.40e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGkatDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15532     1 FCRVCK---DGGELLCCDGCPSSYHLHCLNPPLAEIPDGDWFCPRC 43

PHD2_PHF10

cd15529

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

1010-1055

9.32e-10

Pssm-ID: 277004 Cd Length: 44 Bit Score: 56.93 E-value: 9.32e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDppLQTVPKGGWKCKWC 1055
Cdd:cd15529     1 TCTKCGDPHDEDKMMFCDQCDRGYHTFCVG--LRSIPDGRWICPLC 44

PHA03307

transcriptional regulator ICP4; Provisional

1888-2299

1.12e-09

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 65.19 E-value: 1.12e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1888 AQTSQPPSPQVFSPGSSNSRPPSPMDPYAKMVGTPRPPPVGHSFSRRNSAAPVENCTPLS-SVSRPLQMNETTANRPSPV 1966
Cdd:PHA03307  110 GPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSrQAALPLSSPEETARAPSSP 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1967 RdlcSSSTTNNDPYAKPPDTPRPvmtdQFPKSLGLSRSPVVSEQTAKGPIAAGTSDHFTKPSPRADVFQRQRIPDSYARP 2046
Cdd:PHA03307  190 P---AEPPPSTPPAAASPRPPRR----SSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAP 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2047 LLTPAPLDSGPGPFKTPMQPPPSSqdpygsvSQASRRlsvdpyerpALTPRPidnfshnQSNDPYSQPPLTPHPAVnesf 2126
Cdd:PHA03307  263 ITLPTRIWEASGWNGPSSRPGPAS-------SSSSPR---------ERSPSP-------SPSSPGSGPAPSSPRAS---- 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2127 ahPSRAFSQPGTISRPTSQDPYSQPPGTPRpvvdsySQSSGTARSNTDPYSQPPGTPRPttvdpysqQPQTPRPSTQTdl 2206
Cdd:PHA03307  316 --SSSSSSRESSSSSTSSSSESSRGAAVSP------GPSPSRSPSPSRPPPPADPSSPR--------KRPRPSRAPSS-- 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2207 fvtpvtnqrhsdPYAHPPGTPRPGISvpySQPPATPRPRISEGFTRSSMTRPVlmpnqdPFLQAAQNRGPALPGPLVRPp 2286
Cdd:PHA03307  378 ------------PAASAGRPTRRRAR---AAVAGRARRRDATGRFPAGRPRPS------PLDAGAASGAFYARYPLLTP- 435

                         410
                  ....*....|....*..
gi 578814480 2287 dtcSQTP----RPPGPG 2299
Cdd:PHA03307  436 ---SGEPwpgsPPPPPG 449

PHD_BAZ1B

cd15628

PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...

1011-1055

1.25e-09

Pssm-ID: 277098 Cd Length: 46 Bit Score: 56.68 E-value: 1.25e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15628     2 CKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC 46

PHD1_AIRE

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

1007-1055

2.32e-09

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

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 55.53 E-value: 2.32e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480 1007 ECTVCeacgkaTDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15539     1 ECAVC------GDGGELLCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43

PHD_PHF21A

cd15523

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

1010-1055

2.37e-09

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

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 55.48 E-value: 2.37e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1010 VCEACGKAtdpGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15523     1 FCSVCRKS---GELLMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43

PHD1_KDM5A

cd15602

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...

391-436

2.83e-09

Pssm-ID: 277075 Cd Length: 49 Bit Score: 55.73 E-value: 2.83e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15602     1 VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKC 46

PHD_PHRF1

cd15536

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

392-436

2.91e-09

Pssm-ID: 277011 Cd Length: 46 Bit Score: 55.50 E-value: 2.91e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15536     2 CEVCGRSDREDRLLLCDGCDAGYHMECLTPPLDEVPIEEWFCPEC 46

ePHD_PHF11

cd15712

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...

4473-4554

3.10e-09

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: 57.60 E-value: 3.10e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4473 DLWVHLNCALWSTEVYETQAGALINVELA---------LRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCAIKAQCMF 4543
Cdd:cd15712    20 NIAAHQNCLLYSSGFVESEEYNPLNLDRRfdvesvlneIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALCDDAAI 99

                          90
                  ....*....|....*.
gi 578814480 4544 FKDKT-----MLCPMH 4554
Cdd:cd15712   100 ETDEVrgiyrVFCQKH 115

PHD2_PHF14

cd15562

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

1010-1055

4.04e-09

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

Pssm-ID: 277037 Cd Length: 50 Bit Score: 55.10 E-value: 4.04e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKG----GWKCKWC 1055
Cdd:cd15562     1 SCGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTRMPKKtknsGWQCSEC 50

PHD1_KDM5B

cd15603

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis ...

391-436

5.01e-09

Pssm-ID: 277076 Cd Length: 46 Bit Score: 54.96 E-value: 5.01e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15603     1 VCLVCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC 46

PHD_SF

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

1010-1055

6.15e-09

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: 54.63 E-value: 6.15e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480 1010 VCEACGKATD-PGRLLLCDDCDISYHTYCLDPPLQT-VPKGGWKCKWC 1055
Cdd:cd15489     1 SCIVCGKGGDlGGELLQCDGCGKWFHADCLGPPLSSfVPNGKWICPVC 48

PHD

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

345-392

6.83e-09

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 54.42 E-value: 6.83e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 578814480   345 CAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAVT--PLKRAGWQCPECKVC 392
Cdd:pfam00628    2 CAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDpaEIPSGEWLCPECKPK 51

PHA03307

transcriptional regulator ICP4; Provisional

1894-2282

7.49e-09

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 62.50 E-value: 7.49e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1894 PSPQVFSPGSSNSRPPSPMDPYAKMVGTPRPPPVGHSFSRRNSAAPVEN------CTPLSS------------VSRPLQM 1955
Cdd:PHA03307   99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpaasppAAGASPaavasdaassrqAALPLSS 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1956 NETTANRPSPVRdlcSSSTTNNDPYAKPPDTPRPvmtdQFPKSLGLSRSPVVSEQTAKGPIAAGTSDHFTKPSPRADVFQ 2035
Cdd:PHA03307  179 PEETARAPSSPP---AEPPPSTPPAAASPRPPRR----SSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGP 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2036 RQRIPDSYARPLLTPAPLDSGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSNDPYSqpP 2115
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS--T 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2116 LTPHPAVNESFAHPSRAFSQPGTISRPTSQDPYSQPP--GTPRPVVDSYSQSSGTARSNTDPYSQ-PPGTPRPTTvdpyS 2192
Cdd:PHA03307  330 SSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRkrPRPSRAPSSPAASAGRPTRRRARAAVaGRARRRDAT----G 405

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2193 QQPQTPRPSTQTDLFVTPvtnqrhSDPYAHPP-----GTPRPGisvpySQPPATPRPRisegFTRSSMTRPVLMpnQDPF 2267
Cdd:PHA03307  406 RFPAGRPRPSPLDAGAAS------GAFYARYPlltpsGEPWPG-----SPPPPPGRVR----YGGLGDSRPGLW--DAPE 468

                         410
                  ....*....|....*
gi 578814480 2268 LQAAQNRGPALPGPL 2282
Cdd:PHA03307  469 VREAAARYEASPGPV 483

PHD1_Lid2p_like

cd15519

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

391-436

8.07e-09

Pssm-ID: 276994 [Multi-domain] Cd Length: 46 Bit Score: 54.39 E-value: 8.07e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15519     1 GCEVCGLDDNEGEVLLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC 46

PHA03307

transcriptional regulator ICP4; Provisional

1968-2375

9.89e-09

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 62.11 E-value: 9.89e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1968 DLCSSSTTNNDPYAKPPDTPRPVMTDQF---PKSLGLSRSPVVSEQTAKGPIAAGTSDHFTKPSPRAdvfqRQRIPDSYA 2044
Cdd:PHA03307    9 DLIEAAAEGGEFFPRPPATPGDAADDLLsgsQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGP----GTEAPANES 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2045 RPLLTPAPLDSGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSNDPYSQPPLTPHPAVNE 2124
Cdd:PHA03307   85 RSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2125 SFAHP-------------SRAFSQPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDP- 2190
Cdd:PHA03307  165 DAASSrqaalplsspeetARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSEs 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2191 ----YSQQPQTPRPSTQTDLFVTPVTNQRHSDPYA--HPPGTPRPGISVPYSQP--------PATPRPRISEGFTRSSmt 2256
Cdd:PHA03307  245 sgcgWGPENECPLPRPAPITLPTRIWEASGWNGPSsrPGPASSSSSPRERSPSPspsspgsgPAPSSPRASSSSSSSR-- 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2257 rpvlmpnqDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPGPglSDTFSRVSPSAARDPYDQSPMTPRSQSDSFGtSQTA 2336
Cdd:PHA03307  323 --------ESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP--PPPADPSSPRKRPRPSRAPSSPAASAGRPTR-RRAR 391

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 578814480 2337 HDVADQPRP-GSEGSFCASSNSPMHSQGQQFSGVSQLPGP 2375
Cdd:PHA03307  392 AAVAGRARRrDATGRFPAGRPRPSPLDAGAASGAFYARYP 431

ePHD_PHF6_like

cd15673

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...

250-331

1.03e-08

Pssm-ID: 277143 Cd Length: 116 Bit Score: 56.25 E-value: 1.03e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  250 CWAHHRCVEWSLGVCQMEEPLLVN--------VDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAG---TF 318
Cdd:cd15673    23 IAAHHNCMLFSSGLVQYVSPNENDfggfdiedVKKEIKRGRKLKCNLCKKTGATIGCDVKQCKKTYHYHCAKKDDakiIE 102

                          90
                  ....*....|....
gi 578814480  319 QDFSHIF-LLCPEH 331
Cdd:cd15673   103 RNSQGIYrVYCKNH 116

dnaA

PRK14086

chromosomal replication initiator protein DnaA;

2045-2240

1.52e-08

chromosomal replication initiator protein DnaA;

Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 60.99 E-value: 1.52e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2045 RPLLTPAPLDSGPGPFKTPMQPPPSSQDPYGSvsqASRRLSVDPYERPALTPRPidnfshnQSNDPYSQPPlTPHPAV-- 2122
Cdd:PRK14086   80 RPIRIAITVDPSAGEPAPPPPHARRTSEPELP---RPGRRPYEGYGGPRADDRP-------PGLPRQDQLP-TARPAYpa 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2123 ----NESFAHPSRAFSQPGTISR--PTSQDPYSqPPGTPRPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQ 2196
Cdd:PRK14086  149 yqqrPEPGAWPRAADDYGWQQQRlgFPPRAPYA-SPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTD 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 2197 TPRPStqtdlfvtPVTNQRH--SDPYAHPPGTPRPGISVPYSQPPA 2240
Cdd:PRK14086  228 RPEPP--------PGAGHVHrgGPGPPERDDAPVVPIRPSAPGPLA 265

PHD2_d4

cd15530

PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three ...

392-436

1.63e-08

Pssm-ID: 277005 Cd Length: 46 Bit Score: 53.16 E-value: 1.63e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15530     2 CSLCGTSENDDQLLFCDDCDRGYHMYCLSPPMSEPPEGSWSCHLC 46

PHD_BAZ2A

cd15629

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

1011-1056

1.82e-08

Pssm-ID: 277099 Cd Length: 47 Bit Score: 53.32 E-value: 1.82e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1056
Cdd:cd15629     2 CLVCRKGDNDEYLLLCDGCDRGCHMYCHRPKMLQVPEGDWFCPNCV 47

Atrophin-1

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

1874-2229

2.12e-08

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 60.94 E-value: 2.12e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  1874 PAPSRIPIQDSLSQAQTSQPPSPQVFSPGSS--NSRPP-------SPM---------------DPYAKMVGTPRPPPvgh 1929
Cdd:pfam03154  181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSpaTSQPPnqtqstaAPHtliqqtptlhpqrlpSPHPPLQPMTQPPP--- 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  1930 sfSRRNSAAPVENC---TPLSSVSRPLQMNETTANRPSPVRDLCSSSTTNNDPYAKPPDTPRPVMTDQFPKSLGLSRSPV 2006
Cdd:pfam03154  258 --PSQVSPQPLPQPslhGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQ 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2007 VSEQTAKGPI-AAGTSDHFTKPSPRADVFQRQRiPDSYARPlltpaPLDSGPGPFKTPMQ-PPPSSQDPYGSVSQasrrl 2084
Cdd:pfam03154  336 SQQPPREQPLpPAPLSMPHIKPPPTTPIPQLPN-PQSHKHP-----PHLSGPSPFQMNSNlPPPPALKPLSSLST----- 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2085 svdpYERPALTPRPIDNFSHNQsndPYSQPPLTPhPAVNESFAHPSRAFSQP--GTISRPTSQDPYSQ---PPGTPRPVV 2159
Cdd:pfam03154  405 ----HHPPSAHPPPLQLMPQSQ---QLPPPPAQP-PVLTQSQSLPPPAASHPptSGLHQVPSQSPFPQhpfVPGGPPPIT 476

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2160 DsySQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRHSDPyaHPPGTPRP 2229
Cdd:pfam03154  477 P--PSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPP--PPPRSPSP 542

PHD_SF

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

389-436

2.15e-08

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 53.09 E-value: 2.15e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  389 CKVCQNCKQSGEDskMLVCDTCDKGYHTFCLQPVMKS-VPTNGWKCKNC 436
Cdd:cd15489     2 CIVCGKGGDLGGE--LLQCDGCGKWFHADCLGPPLSSfVPNGKWICPVC 48

ePHD_TCF20

cd15699

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...

251-331

2.64e-08

Pssm-ID: 277169 Cd Length: 103 Bit Score: 54.54 E-value: 2.64e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  251 WAHHRCVEWSLGVcQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLLCPE 330
Cdd:cd15699    24 WVHEGCILWANGI-YLVCGRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLNEENFSVRCPK 102


                  .
gi 578814480  331 H 331
Cdd:cd15699   103 H 103

PHD_UHRF1_2

cd15525

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...

389-436

3.69e-08

Pssm-ID: 277000 Cd Length: 47 Bit Score: 52.37 E-value: 3.69e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  389 CKVCQNcKQsgEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNG-WKCKNC 436
Cdd:cd15525     2 CHVCGG-KQ--DPEKQLLCDECDMAYHLYCLDPPLTSLPDDDeWYCPDC 47

PHD1_PHF12

cd15533

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

1010-1055

3.80e-08

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

Pssm-ID: 277008 [Multi-domain] Cd Length: 45 Bit Score: 52.36 E-value: 3.80e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480 1010 VCEACGkatDPGRLLLCDDCDISYHTYCLDPPL--QTVPKGGWKCKWC 1055
Cdd:cd15533     1 YCDSCG---EGGDLLCCDRCPASFHLQCCNPPLdeEDLPPGEWLCHRC 45

PHD_SF

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

960-1008

4.15e-08

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 52.32 E-value: 4.15e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  960 MCVVCGSFGQGaEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLEC 1008
Cdd:cd15489     1 SCIVCGKGGDL-GGELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48

PHD_SF

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

468-518

4.28e-08

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 52.32 E-value: 4.28e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  468 CPFCGKCYHPElqKDMLHCNMCKRWVHLECDKPTDHELDTqlKEEYICMYC 518
Cdd:cd15489     2 CIVCGKGGDLG--GELLQCDGCGKWFHADCLGPPLSSFVP--NGKWICPVC 48

PHD3_KMT2A

cd15592

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

467-518

8.85e-08

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.

Pssm-ID: 277067 Cd Length: 57 Bit Score: 51.53 E-value: 8.85e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480  467 LCPFCGKCYHP-ELQKDMLHCNMCKRWVHLECDKPTD--HELDTQLKEE--YICMYC 518
Cdd:cd15592     1 FCPLCDKCYDDdDYESKMMQCGKCDRWVHSKCENLSDemYEILSNLPESvaYTCINC 57

PHD3_PHF14

cd15563

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

1007-1055

8.95e-08

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

Pssm-ID: 277038 Cd Length: 49 Bit Score: 51.24 E-value: 8.95e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578814480 1007 ECTVCEACGKATDpgrLLLCDDCDISYHTYCLDPPLQTVPKG---GWKCKWC 1055
Cdd:cd15563     1 ECCVCKQTGDNSQ---LVRCDECKLCYHFGCLDPPLKKSPKQrgyGWVCEEC 49

SET_Suv4-20-like

cd10524

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

4817-4956

9.56e-08

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

Pssm-ID: 380922 [Multi-domain] Cd Length: 141 Bit Score: 54.21 E-value: 9.56e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4817 WKSNVYLARSRiQGLGLYAARDIEKHTMVIEYIGTIIRNEVAnrkEKLYESQNRG----VYMFRMDNDHVIDatltgGPA 4892
Cdd:cd10524     7 CPCNRYSLENH-YGAKIIATKPIKKGEKIHELCGCIAELSEE---EEALLRPGGNdfsvMYSSRKKCSQLWL-----GPA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578814480 4893 RYINHSCAPNCvaEVVTFERGhKIIISSSRRIQKGEELCYDYKFDFEDDQHkipCHCGAVNCRK 4956
Cdd:cd10524    78 AFINHDCRPNC--KFVPTGKS-TACVKVLRDIEPGEEITVYYGDNYFGENN---EECECETCER 135

PHA03378

EBNA-3B; Provisional

2048-2447

1.39e-07

EBNA-3B; Provisional

Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 58.15 E-value: 1.39e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2048 LTPAPldsGPGPFKtpMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSN-DPYSQP-PLTPHPAvnes 2125
Cdd:PHA03378  563 LLPAP---GLGPLQ--IQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETsAPRQWPmPLRPIPM---- 633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2126 faHPSRAfsQPGTISRPTSQDPYSQPPGTPRPVVDSYSQssgTARSNTDPYSQPPGTPRPTTVDPYSQQPQTPRPSTQTD 2205
Cdd:PHA03378  634 --RPLRM--QPITFNVLVFPTPHQPPQVEITPYKPTWTQ---IGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRP 706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2206 LFVTPVTNQRhsdPYAHPPGTPRPGISVPYSQPP-ATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVr 2284
Cdd:PHA03378  707 PAAPPGRAQR---PAAATGRARPPAAAPGRARPPaAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQA- 782

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2285 PPDTCSQ-----TPRPPgPGLSDTFSRVSPSAArdPYDQSPMT---------------PRSQSDSFGTSQTAhdVADQPR 2344
Cdd:PHA03378  783 PPAPQQRprgapTPQPP-PQAGPTSMQLMPRAA--PGQQGPTKqilrqlltggvkrgrPSLKKPAALERQAA--AGPTPS 857

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2345 PGSeGSFCASSNSPMH----SQGQQFSGVSQLPGPVPTSGVTdtqntvnmaQADTEKLRQRqklREIILQQQQQKKIAGR 2420
Cdd:PHA03378  858 PGS-GTSDKIVQAPVFyppvLQPIQVMRQLGSVRAAAASTVT---------QAPTEYTGER---RGVGPMHPTDIPPSKR 924

                         410       420
                  ....*....|....*....|....*....
gi 578814480 2421 QEKGSQDSPAVPHPGPLQHWQP--ENVNQ 2447
Cdd:PHA03378  925 AKTDAYVESQPPHGGQSHSFSViwENVSQ 953

PHD1_CHD_II

cd15531

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

392-436

1.49e-07

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

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 50.68 E-value: 1.49e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEdskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15531     2 CEVCQQGGE---IILCDTCPRAYHLVCLDPELEKAPEGKWSCPHC 43

PHD_SF

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

1087-1137

1.50e-07

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 50.78 E-value: 1.50e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1087 SCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVadiGFDCSMC 1137
Cdd:cd15489     1 SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNG---KWICPVC 48

PHA03379

EBNA-3A; Provisional

1888-2349

1.65e-07

EBNA-3A; Provisional

Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 58.15 E-value: 1.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1888 AQTSQPPSPQVFSPGSSNSR-----------PPSPMDPYAKMVGTPRPPPVGhsfsrRNSAAPVEncTPLSSVSRPLQMN 1956
Cdd:PHA03379  440 AQVPEPPPVHDLEPGPLHDQhsmapcpvaqlPPGPLQDLEPGDQLPGVVQDG-----RPACAPVP--APAGPIVRPWEAS 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1957 ETTANRPSPvrdlcssSTTNNDPYAKPPDtPRPVMTDQFPKslglsrSPVVSEQTAKGPIAAGTSdhftkpspradvfqr 2036
Cdd:PHA03379  513 LSQVPGVAF-------APVMPQPMPVEPV-PVPTVALERPV------CPAPPLIAMQGPGETSGI--------------- 563

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2037 QRIPDSYARPLLTPAPLDSgpgPFKTPMQPPPSSQDPYGSVSQASrrLSVDPYERPALTPrpidnfshnqsndpysQPPL 2116
Cdd:PHA03379  564 VRVRERWRPAPWTPNPPRS---PSQMSVRDRLARLRAEAQPYQAS--VEVQPPQLTQVSP----------------QQPM 622

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2117 TpHPAVNESFAHPSRAFSQPGTISRpTSQDPYSQPPGTPRPVVDSYSQSSGTA--RSNTDPYSqppgtPRPTTVDPYSQQ 2194
Cdd:PHA03379  623 E-YPLEPEQQMFPGSPFSQVADVMR-AGGVPAMQPQYFDLPLQQPISQGAPLAplRASMGPVP-----PVPATQPQYFDI 695

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2195 PQTPRPSTQTDLFvtpvtnqrHSDPYAhpPGTprpgisvpysqPPATPRPRISEGFTRSSMTRPVLMPNQD---PFLQAA 2271
Cdd:PHA03379  696 PLTEPINQGASAA--------HFLPQQ--PME-----------GPLVPERWMFQGATLSQSVRPGVAQSQYfdlPLTQPI 754

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2272 QNRGPALPGPlvrppdtcsqtPRPPGPGlsdtfsrvSPSAARDPYDQSPMTPRS-----QSDSFGtsQTAHDVADQPRPG 2346
Cdd:PHA03379  755 NHGAPAAHFL-----------HQPPMEG--------PWVPEQWMFQGAPPSQGTdvvqhQLDALG--YVLHVLNHPGVPV 813


                  ...
gi 578814480 2347 SEG 2349
Cdd:PHA03379  814 SPA 816

PHD3_KMT2A_like

cd15508

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

1087-1137

1.80e-07

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

Pssm-ID: 276983 Cd Length: 57 Bit Score: 50.91 E-value: 1.80e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578814480 1087 SCPVCYRNYREEDL---ILQCRQCDRWMHAVCQNLnTEEEVENVAD----IGFDCSMC 1137
Cdd:cd15508     1 YCPLCEKCYDDDDYdskMMQCSQCDHWVHAKCEGL-SDEMYEILSYlpesIEYTCSLC 57

PHD_PHF21A

cd15523

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

391-436

2.10e-07

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 50.09 E-value: 2.10e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEdskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15523     1 FCSVCRKSGE---LLMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43

PHD_BAZ2B

cd15630

PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also ...

1011-1056

2.31e-07

PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also termed WALp4, is a bromodomain-containing protein whose biological role is still elusive. It shows high sequence similarly with BAZ2A, which is the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP-and histone H4 tail-dependent fashion. BAZ2B contains a TAM (TIP5/ARBP/MBD) domain, an Apolipophorin-III like domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain.

Pssm-ID: 277100 Cd Length: 49 Bit Score: 50.36 E-value: 2.31e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1056
Cdd:cd15630     3 CQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPEGDWFCPACI 48

PHD1_CHD_II

cd15531

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

1011-1055

2.34e-07

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 49.91 E-value: 2.34e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKAtdpGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15531     2 CEVCQQG---GEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHC 43

PHD_TIF1_like

cd15541

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

1007-1055

2.42e-07

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

Pssm-ID: 277016 [Multi-domain] Cd Length: 43 Bit Score: 50.04 E-value: 2.42e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480 1007 ECTVCEacgkatDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15541     1 WCAVCQ------NGGELLCCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC 43

PHD_BAZ2B

cd15630

PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also ...

392-436

2.89e-07

Pssm-ID: 277100 Cd Length: 49 Bit Score: 49.97 E-value: 2.89e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15630     3 CQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPEGDWFCPAC 47

PHD

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

468-518

2.91e-07

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 49.90 E-value: 2.91e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 578814480    468 CPFCGKCYHPElqkDMLHCNMCKRWVHLECDKPTDHELDtqLKEEYICMYC 518
Cdd:smart00249    2 CSVCGKPDDGG---ELLQCDGCDRWYHQTCLGPPLLEEE--PDGKWYCPKC 47

PHD3_PHF14

cd15563

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

391-436

3.11e-07

Pssm-ID: 277038 Cd Length: 49 Bit Score: 49.70 E-value: 3.11e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTN---GWKCKNC 436
Cdd:cd15563     1 ECCVCKQTGDNSQLVRCDECKLCYHFGCLDPPLKKSPKQrgyGWVCEEC 49

PHA03378

EBNA-3B; Provisional

1886-2394

4.19e-07

EBNA-3B; Provisional

Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 56.61 E-value: 4.19e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1886 SQAQT---SQPPSPQVFSPGSSnSRPPSPMDPYAKMVGTPRPPPVGHSFSRRNSAAPVENCTPLSSVSRPLQMN------ 1956
Cdd:PHA03378  447 SQAPTvvlHRPPTQPLEGPTGP-LSVQAPLEPWQPLPHPQVTPVILHQPPAQGVQAHGSMLDLLEKDDEDMEQRvmatll 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1957 ETTANRPSPVRDLCSSSTTNNDPYAKPPDTPRPVMtDQFPKSLGLS-------RSPVVSEQTAKGPIAAGTSDHFTKPSP 2029
Cdd:PHA03378  526 PPSPPQPRAGRRAPCVYTEDLDIESDEPASTEPVH-DQLLPAPGLGplqiqplTSPTTSQLASSAPSYAQTPWPVPHPSQ 604

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2030 RADVFQRQRIPDSYARPLLTPAPLDSGPGP-------------FKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTP 2096
Cdd:PHA03378  605 TPEPPTTQSHIPETSAPRQWPMPLRPIPMRplrmqpitfnvlvFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTM 684

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2097 RPIdNFSHNQSNDPYSQPPLTPHPAVNESFAHPSRAFSQPG--TISRPTSQDPYSQPPGTPRP--VVDSYSQSSGTARSN 2172
Cdd:PHA03378  685 LPI-QWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRArpPAAAPGRARPPAAAPGRARPpaAAPGRARPPAAAPGR 763

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2173 TDPYSQPPGTPRPT---TVDPYS-QQPQ---TPRPSTQ---TDLFVTPVTNQRHSDPYAHPPGTP--------RPGISVP 2234
Cdd:PHA03378  764 ARPPAAAPGAPTPQpppQAPPAPqQRPRgapTPQPPPQagpTSMQLMPRAAPGQQGPTKQILRQLltggvkrgRPSLKKP 843

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2235 YS---QPPATPRPRISEGFTRSSMTRPVLMPnqdPFLQAAQnrgpaLPGPLVRP-PDTCSQTPRPPgpglsDTFSRVSPS 2310
Cdd:PHA03378  844 AAlerQAAAGPTPSPGSGTSDKIVQAPVFYP---PVLQPIQ-----VMRQLGSVrAAAASTVTQAP-----TEYTGERRG 910

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2311 AARDPYDQSPMTPRSQSDSFGTSQTAHdvadqprpgsegsfcassNSPMHSQGQQFSGVSQLPGPVPTSGVTDTQNTVNM 2390
Cdd:PHA03378  911 VGPMHPTDIPPSKRAKTDAYVESQPPH------------------GGQSHSFSVIWENVSQGQQQTLECGGTTKQERAML 972


                  ....
gi 578814480 2391 AQAD 2394
Cdd:PHA03378  973 GTGD 976

PHD_SF

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

345-389

5.20e-07

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 49.24 E-value: 5.20e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480  345 CAVCDSPGDLLDQF-FCTTCGQHYHGMCLDIAVTPL-KRAGWQCPEC 389
Cdd:cd15489     2 CIVCGKGGDLGGELlQCDGCGKWFHADCLGPPLSSFvPNGKWICPVC 48

PHD

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

345-389

5.30e-07

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 49.13 E-value: 5.30e-07

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578814480    345 CAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAVTP-LKRAGWQCPEC 389
Cdd:smart00249    2 CSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD2_PHF14

cd15562

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

391-436

9.38e-07

Pssm-ID: 277037 Cd Length: 50 Bit Score: 48.56 E-value: 9.38e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVP----TNGWKCKNC 436
Cdd:cd15562     1 SCGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTRMPkktkNSGWQCSEC 50

PHD1_MTF2_PHF19_like

cd15499

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...

1010-1061

1.24e-06

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

Pssm-ID: 276974 Cd Length: 53 Bit Score: 48.27 E-value: 1.24e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578814480 1010 VCEACG--KATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKcKWcvWCRHC 1061
Cdd:cd15499     1 TCSICGgaEARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGDE-KW--FCSRC 51

PHD

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

468-519

1.42e-06

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 47.87 E-value: 1.42e-06

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480   468 CPFCGKcyhPELQKDMLHCNMCKRWVHLECDKPTDhELDTQLKEEYICMYCK 519
Cdd:pfam00628    2 CAVCGK---SDDGGELVQCDGCDDWFHLACLGPPL-DPAEIPSGEWLCPECK 49

PHD1_Rco1

cd15535

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

1011-1055

1.51e-06

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

Pssm-ID: 277010 [Multi-domain] Cd Length: 45 Bit Score: 47.80 E-value: 1.51e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 1011 CEACGKatdPGRLLLCDDCDISYHTYCLDPPL--QTVPKGGWKCKWC 1055
Cdd:cd15535     2 CSACGG---YGSFLCCDGCPRSFHFSCLDPPLeeDNLPDDEWFCNEC 45

PHD_ARID4_like

cd15615

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...

467-518

1.71e-06

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

Pssm-ID: 277087 Cd Length: 57 Bit Score: 47.86 E-value: 1.71e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480  467 LCPFCGKCYHP--ELQKDMLHCNMCKRWVHLECDKPT--DHELDTQLKE-EYICMYC 518
Cdd:cd15615     1 FCILCGQVYEEneGDEKEWVQCDSCSEWVHFECDGRTglGAFKYAKSDGlQYVCPRC 57

HMG-box_SF

cd00084

high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found ...

1672-1719

2.00e-06

high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found in a variety of eukaryotic chromosomal proteins and transcription factors. HMGs bind to the minor groove of DNA and have been classified by DNA binding preferences. Two phylogenetically distinct groups of Class I proteins bind DNA in a sequence specific fashion and contain a single HMG box. One group (SOX-TCF) includes transcription factors, TCF-1, -3, -4, and also SRY and LEF-1, which bind four-way DNA junctions and duplex DNA targets. The second group (MATA) includes fungal mating type gene products MC, MATA1 and Ste11. Class II and III proteins (HMGB-UBF) bind DNA in a non-sequence specific fashion and contain two or more tandem HMG boxes. Class II members include non-histone chromosomal proteins, HMG1 and HMG2, which bind to bent or distorted DNA such as four-way DNA junctions, synthetic DNA cruciforms, kinked cisplatin-modified DNA, DNA bulges, cross-overs in supercoiled DNA, and can cause looping of linear DNA. Class III members include nucleolar and mitochondrial transcription factors, UBF and mtTF1, which bind four-way DNA junctions.

Pssm-ID: 438789 [Multi-domain] Cd Length: 59 Bit Score: 47.90 E-value: 2.00e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480 1672 LYTNINFPNLKEEFPDWTTR--VKQIAKLWRKASSQERAPYVQKARDNRA 1719
Cdd:cd00084     8 LFSKEKRPKLKKENPDLSFTeiSKLLGERWKELSEEEKQPYEEKAKEDKE 57

PHA03377

EBNA-3C; Provisional

2062-2566

2.04e-06

EBNA-3C; Provisional

Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 54.67 E-value: 2.04e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2062 TPMQPPPSSQDPygsvsqasrrlsvDPYERPALTPRpidnfshNQSNDPYSQPPLTPHPAVNESFAHPSRAFSQP----- 2136
Cdd:PHA03377  449 TPERPGPSDQPS-------------VPVEPAHLTPV-------EHTTVILHQPPQSPPTVAIKPAPPPSRRRRGAcvvyd 508

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2137 ----GTISRPTSQD--PYSQPPGTPRPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQTPRPSTQTDLFVTP 2210
Cdd:PHA03377  509 ddiiEVIDVETTEEeeSVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPR 588

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2211 VTNQRHSDPYAHPPGTPRPGISVPYSQPPATPRPRISEGFTRSSMTRPVLMP----------------------NQDPfl 2268
Cdd:PHA03377  589 DMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAPSVVRMFLRERLLEqstgpkpksfwemragrdgsgiQQEP-- 666

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2269 qaAQNRGPALPGPLVRP---PDTCSQTPRPPGPGLSDTFSRVSPSAARDPydqspmTPRSQSDSFGTSQTAHDVADQPrp 2345
Cdd:PHA03377  667 --SSRRQPATQSTPPRPswlPSVFVLPSVDAGRAQPSEESHLSSMSPTQP------ISHEEQPRYEDPDDPLDLSLHP-- 736

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2346 gsegsfcasSNSPMHSQGQQFSGVSQLPGP-VPTSGVTDTQntvnmaqadteklrqrqklreiilqqQQQKKIAGRQEKG 2424
Cdd:PHA03377  737 ---------DQAPPPSHQAPYSGHEEPQAQqAPYPGYWEPR--------------------------PPQAPYLGYQEPQ 781

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2425 SQDSPAVPHPGPLQHWQPENVNQAFTRPPPPYPgniRSPV-APPLGPRyavfpkDQRGPYPPDVASmgmrphgfrfGFPG 2503
Cdd:PHA03377  782 AQGVQVSSYPGYAGPWGLRAQHPRYRHSWAYWS---QYPGhGHPQGPW------APRPPHLPPQWD----------GSAG 842

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578814480 2504 GSHgTMPSQerflVPPQQIQGSGVSPQLRRSVSVDMPRPLNNS--------QMNNPV-GLPQHFSPQSLPVQ 2566
Cdd:PHA03377  843 HGQ-DQVSQ----FPHLQSETGPPRLQLSQVPQLPYSQTLVSSsapswsspQPRAPIrPIPTRFPPPPMPLQ 909

PHD1_AIRE

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

392-436

2.18e-06

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 47.06 E-value: 2.18e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEdskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15539     2 CAVCGDGGE---LLCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43

SET_SpSet7-like

cd10540

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

4821-4940

2.36e-06

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

Pssm-ID: 380938 Cd Length: 112 Bit Score: 49.17 E-value: 2.36e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4821 VYLARSRIQGLGLYAARDIEKHTmVIEYIGTIIrneVANRKEKLYESQNRGVYMFRMDNDHVidATLTGGPARYiNHSCA 4900
Cdd:cd10540     2 LEVKPSTLKGRGVFATRPIKKGE-VIEEAPVIV---LPKEEYQHLCKTVLDHYVFSWGDGCL--ALALGYGSMF-NHSYT 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 578814480 4901 PNcvAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFED 4940
Cdd:cd10540    75 PN--AEYEIDFENQTIVFYALRDIEAGEELTINYGDDLWD 112

zf-HC5HC2H_2

pfam13832

PHD-zinc-finger like domain;

251-331

3.06e-06

PHD-zinc-finger like domain;

Pssm-ID: 463991 [Multi-domain] Cd Length: 109 Bit Score: 48.88 E-value: 3.06e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480   251 WAHHRCVEWSLGVC-----QMEeplLVNVDKAVVSGSTERCAFCKHL-GATIKCCEEKCTQMYHYPCAAGAGTFQDFSHI 324
Cdd:pfam13832   21 WVHVLCAIFVPEVRfgnvaTME---PIDVSRIPPERWKLKCVFCKKRsGACIQCSKGRCTTAFHVTCAQAAGVYMEPEDW 97

                           90
                   ....*....|..
gi 578814480   325 -----FLLCPEH 331
Cdd:pfam13832   98 pnvvvIAYCQKH 109

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

961-1008

4.07e-06

Pssm-ID: 276984 Cd Length: 48 Bit Score: 46.53 E-value: 4.07e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480  961 CVVCGSFGQGAEgrLLACSQCGQCYHPYCV--SIKITKVVLSkGWRCLEC 1008
Cdd:cd15509     2 CAVCDSPGDLSD--LLFCTSCGQHYHGSCLdpAVRPTPLVRA-GWQCPEC 48

PHD3_KMT2A_like

cd15508

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

467-518

4.19e-06

Pssm-ID: 276983 Cd Length: 57 Bit Score: 47.06 E-value: 4.19e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480  467 LCPFCGKCYH-PELQKDMLHCNMCKRWVHLECDKPTD--HELDTQLKE--EYICMYC 518
Cdd:cd15508     1 YCPLCEKCYDdDDYDSKMMQCSQCDHWVHAKCEGLSDemYEILSYLPEsiEYTCSLC 57

PHD1_BPTF

cd15559

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

1011-1055

4.54e-06

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

Pssm-ID: 277034 [Multi-domain] Cd Length: 43 Bit Score: 46.25 E-value: 4.54e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKAtdpGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15559     2 CRVCHKL---GDLLCCETCSAVYHLECVDPPLEEVPEEDWQCEVC 43

PRK07764

DNA polymerase III subunits gamma and tau; Validated

1888-2244

4.85e-06

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 53.07 E-value: 4.85e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1888 AQTSQPPSPQVFSPGSSNSRPPSPmDPYAKMVGTPRPPPVGHSFSRRNSAAPVENCTPLSSVSRPLQMNEttANRPSPVR 1967
Cdd:PRK07764  412 PAAAAPAAAAAPAPAAAPQPAPAP-APAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP--APAPPAAP 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1968 DLCSSSTTNNDPYAKPPDTPRPVMTDQFPKSLGL--SRSPVVSEQTAKGPIAAGTSDH-----FTKPsPRADVFQRQRIP 2040
Cdd:PRK07764  489 APAAAPAAPAAPAAPAGADDAATLRERWPEILAAvpKRSRKTWAILLPEATVLGVRGDtlvlgFSTG-GLARRFASPGNA 567

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2041 DSYA-----------RPLLTPAPlDSGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSND 2109
Cdd:PRK07764  568 EVLVtalaeelggdwQVEAVVGP-APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPG 646

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2110 PYSQPPLTPHPAVNESFAHPS---RAFSQPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSN--TDPYSQPPGTPR 2184
Cdd:PRK07764  647 VAAPEHHPKHVAVPDASDGGDgwpAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGqaDDPAAQPPQAAQ 726

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2185 PTTVDPYSQQPQTPRPSTQTDlfvtpvtnqrHSDPYAHPPGTPRPGISVPYSQPPATPRP 2244
Cdd:PRK07764  727 GASAPSPAADDPVPLPPEPDD----------PPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776

PRK10263

DNA translocase FtsK; Provisional

1971-2486

5.00e-06

DNA translocase FtsK; Provisional

Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 53.17 E-value: 5.00e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1971 SSSTTNNDPYAKPPDtprPVM-TDQFPKSLGLSRSPVVSEQTAKGP----------------------IAAGTSDHFTKP 2027
Cdd:PRK10263  324 AAATTATQSWAAPVE---PVTqTPPVASVDVPPAQPTVAWQPVPGPqtgepviapapegypqqsqyaqPAVQYNEPLQQP 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2028 SPRADVFQRQRIPDSYARPLLTPAPLDSGPGPFKTPMQPPPSSQDPYGSVSQASrrlsvdPYErpaltprpidnfshnqs 2107
Cdd:PRK10263  401 VQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQS------TFA----------------- 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2108 NDPYSQPPLT-PHPAVNESFAHPSRAFSQPGTIsRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSNTDPYSQPpgTPRPT 2186
Cdd:PRK10263  458 PQSTYQTEQTyQQPAAQEPLYQQPQPVEQQPVV-EPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQP--IPEPV 534

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2187 TvDPYSQQPQTPRPSTQTdlfVTPVTNQRHSDPYAH--PPGTPRPGISVPYSQPP------ATPRPRISEGFtrssmtrp 2258
Cdd:PRK10263  535 K-EPEPIKSSLKAPSVAA---VPPVEAAAAVSPLASgvKKATLATGAAATVAAPVfslansGGPRPQVKEGI-------- 602

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2259 vlmpnqdpflqaaqnrGPALPGP-LVRPP---DTCSQTPRPPGPGLSDTFSRvspSAARDPYDQSPMTPRSQSDS----- 2329
Cdd:PRK10263  603 ----------------GPQLPRPkRIRVPtrrELASYGIKLPSQRAAEEKAR---EAQRNQYDSGDQYNDDEIDAmqqde 663

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2330 ----FGTSQT-------AHDVADQPRPGSEGSFCASSNSPMHSQGQQFSG----------------------VSQLPG-P 2375
Cdd:PRK10263  664 larqFAQTQQqrygeqyQHDVPVNAEDADAAAEAELARQFAQTQQQRYSGeqpaganpfslddfefspmkalLDDGPHeP 743

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2376 VPTSGVTDTQNTVNMAQADTEKLRQRQKLREIILQQQQQKKIAGRQEKGSQDSPAVPHPGPLQHWQPENVNQAFTRPppp 2455
Cdd:PRK10263  744 LFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP--- 820

                         570       580       590
                  ....*....|....*....|....*....|.
gi 578814480 2456 ypgniRSPVAPPlgPRYAVfPKDQRGPYPPD 2486
Cdd:PRK10263  821 -----QQPVAPQ--PQYQQ-PQQPVAPQPQD 843

PHD2_PHF12_Rco1

cd15534

PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...

1010-1052

5.04e-06

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

Pssm-ID: 277009 Cd Length: 47 Bit Score: 46.19 E-value: 5.04e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578814480 1010 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGG-WKC 1052
Cdd:cd15534     1 VCFKCNRSCRVAPLIQCDYCPLLFHLDCLDPPLTHPPATGrWMC 44

PHD_UHRF1

cd15616

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); ...

392-436

5.50e-06

Pssm-ID: 277088 Cd Length: 47 Bit Score: 46.11 E-value: 5.50e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPT-NGWKCKNC 436
Cdd:cd15616     2 CHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPDdEDWYCPEC 47

SET_SETD5

cd19181

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

4833-4954

5.59e-06

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

Pssm-ID: 380958 Cd Length: 150 Bit Score: 49.24 E-value: 5.59e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4833 LYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDN--DHVIDATLTGGPARYINHSCAPNCVAEVVTF 4910
Cdd:cd19181    21 LRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRPYPFVLFYSKFNgvEMCVDARTFGNDARFIRRSCTPNAEVRHMIA 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 4911 ERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHC--GAVNC 4954
Cdd:cd19181   101 DGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCAChkGNRNC 146

ePHD1_PHF6

cd15710

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

4477-4540

5.75e-06

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: 48.42 E-value: 5.75e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578814480 4477 HLNCALWSTEVYETQAG-------ALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCAI--KAQ 4540
Cdd:cd15710    26 HHKCMLFSSALVSSHSDsenlggfSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCALhdKAQ 98

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

1011-1055

5.91e-06

Pssm-ID: 276984 Cd Length: 48 Bit Score: 46.15 E-value: 5.91e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVP--KGGWKCKWC 1055
Cdd:cd15509     2 CAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVRPTPlvRAGWQCPEC 48

SET_AtSUVH-like

cd10545

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

4845-4934

6.42e-06

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: 50.86 E-value: 6.42e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4845 VIEYIGTIIRNEVANRKEKlyesqnRGVYMFRMDN-------------------------------DHVIDATLTGGPAR 4893
Cdd:cd10545   112 ICEYVGELLDTSEADTRSG------NDDYLFDIDNrqtnrgwdggqrldvgmsdgerssaedeessEFTIDAGSFGNVAR 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 4894 YINHSCAPNCVAEVVTFE----RGHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd10545   186 FINHSCSPNLFVQCVLYDhndlRLPRVMLFAADNIPPLQELTYDY 230

DUF5585

pfam17823

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.

2002-2358

7.52e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.

Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 52.27 E-value: 7.52e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2002 SRSPVVSEQTAKGPIAAGTSDHFTKPS---PRAD--VFQRQRIPDSYARPLLTPAPLDSGPGPFKTPMQPPPSSQDPYGS 2076
Cdd:pfam17823  120 SSSPSSAAQSLPAAIAALPSEAFSAPRaaaCRANasAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAA 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2077 VSQASRRLSVDPYERPALTprpidnfshnqsndpysqpplTPHPAVNESFAHPSRAFSQPGTISRPTSQDPYSQPpGTPR 2156
Cdd:pfam17823  200 SSAPATLTPARGISTAATA---------------------TGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAAL-ATLA 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2157 PVVDSYSQSSGTARSnTDPYSQPPGTPRPTTVDPYSQQPQTP-RPSTQTdlfvtPVTNQRHSDPYAHPPGTPRPGISvPY 2235
Cdd:pfam17823  258 AAAGTVASAAGTINM-GDPHARRLSPAKHMPSDTMARNPAAPmGAQAQG-----PIIQVSTDQPVHNTAGEPTPSPS-NT 330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2236 SQPPATPRPRISEGFTRSSMTRpvlmpnqdpflqaAQNRGPalpgplvrppdTCSQTPRPPGpglsdtfSRVSPSAARDP 2315
Cdd:pfam17823  331 TLEPNTPKSVASTNLAVVTTTK-------------AQAKEP-----------SASPVPVLHT-------SMIPEVEATSP 379

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 578814480  2316 YDQ-SPMTPRSQSDSFGTSQTAHDVADQPRPG--SEGSFCASSNSP 2358
Cdd:pfam17823  380 TTQpSPLLPTQGAAGPGILLAPEQVATEATAGtaSAGPTPRSSGDP 425

PRK07003

DNA polymerase III subunit gamma/tau;

2027-2331

9.37e-06

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 52.16 E-value: 9.37e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2027 PSPRADVFQRQRIPDSYARPLLTPAPLDSGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQ 2106
Cdd:PRK07003  381 PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASAD 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2107 SN--DPYSQPPLTPHPAVNESFAHPSRAFSQPGTisrptsqdPYSQPPGTPRPVVDSYSQSSGTARsNTDPYSQPPGTPR 2184
Cdd:PRK07003  461 SRcdERDAQPPADSGSASAPASDAPPDAAFEPAP--------RAAAPSAATPAAVPDARAPAAASR-EDAPAAAAPPAPE 531

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2185 PTTVDPYSQQPQTPRPSTQTDLFVTPVTNQR-HSDPYAHPPGTPRPGISVPYSQPPATPRPRISEGFTRSSMTRPVLMPN 2263
Cdd:PRK07003  532 ARPPTPAAAAPAARAGGAAAALDVLRNAGMRvSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPN 611

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2264 Q-DPFLQAAQNRGPALPGPLVrPPD-----TCSQTPRPPGPGLSDTFS------RVSPSAARDP---YDQSPMTPRSQSD 2328
Cdd:PRK07003  612 GaARAEQAAESRGAPPPWEDI-PPDdyvplSADEGFGGPDDGFVPVFDsgpddvRVAPKPADAPappVDTRPLPPAIPLD 690


                  ...
gi 578814480 2329 SFG 2331
Cdd:PRK07003  691 AIG 693

HMG_box

pfam00505

HMG (high mobility group) box;

1671-1722

1.29e-05

HMG (high mobility group) box;

Pssm-ID: 459837 [Multi-domain] Cd Length: 68 Bit Score: 45.68 E-value: 1.29e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 578814480  1671 VLYTNINFPNLKEEFPDWTTR--VKQIAKLWRKASSQERAPYVQKARDNRAALR 1722
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62

Atrophin-1

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

2236-2564

1.35e-05

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.69 E-value: 1.35e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2236 SQPPATPRPRISEGFTRSSMTRPVLMpNQDPFLQAAQnrGPALPGPLVRPPDTCSQTPRPPgPGLSDTFSRVSPSAARDP 2315
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQ-TQPPVLQAQS--GAASPPSPPPPGTTQAATAGPT-PSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2316 YDQSPM---------TPRSQSDSFGTSQTAHDVADQPRPGSEGSFCASSNSPMHSQGQQF-----SGVSQLPGPVPTSGV 2381
Cdd:pfam03154  219 NQTQSTaaphtliqqTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMphslqTGPSHMQHPVPPQPF 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2382 TDTQntvNMAQADTEKLRQRQklreiilqqQQQKKIAGRQEKGSQDSPAVPHPGPLQHWQPENVNQAFTRPPPPYP---- 2457
Cdd:pfam03154  299 PLTP---QSSQSQVPPGPSPA---------APGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPipql 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2458 GNIRSPVAPPLGPRYAVFPKDQRGPYPPDVASMGMRPHgfrfGFPGGSH----GTMPSQERFLVPPQQIQGSGVSPQLRR 2533
Cdd:pfam03154  367 PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLST----HHPPSAHppplQLMPQSQQLPPPPAQPPVLTQSQSLPP 442

                          330       340       350
                   ....*....|....*....|....*....|..
gi 578814480  2534 SVSvDMPRPLNNSQMNNPVGLPQH-FSPQSLP 2564
Cdd:pfam03154  443 PAA-SHPPTSGLHQVPSQSPFPQHpFVPGGPP 473

PHD_PHF21B

cd15524

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

1011-1055

1.50e-05

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

Pssm-ID: 276999 [Multi-domain] Cd Length: 43 Bit Score: 44.88 E-value: 1.50e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKAtdpGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15524     2 CAACKRG---GNLQPCGTCPRAYHLDCLDPPLKTAPKGVWVCPKC 43

Atrophin-1

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

1880-2215

1.54e-05

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.69 E-value: 1.54e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  1880 PIQDSLSQAQTSQPPSPQVfsPGSSNSRPPSPmdPYAKMVGTPRPPpvghsfsRRNSAAPVenctplssvsrPLQMNETT 1959
Cdd:pfam03154  299 PLTPQSSQSQVPPGPSPAA--PGQSQQRIHTP--PSQSQLQSQQPP-------REQPLPPA-----------PLSMPHIK 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  1960 ANRPSPVRDLCSSSTTNNDPYAKPPDTPRpvMTDQFPKSLGLsrSPVVSEQTAKGPIAagtsdhftKPSPRADVFQRQRI 2039
Cdd:pfam03154  357 PPPTTPIPQLPNPQSHKHPPHLSGPSPFQ--MNSNLPPPPAL--KPLSSLSTHHPPSA--------HPPPLQLMPQSQQL 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2040 PDSYARPlltpapldsgPGPFKTPMQPPPSSQDPYGSVSQASrrlsvdpyerPALTPRPIDNFSHNQSndPYSQPPLTPH 2119
Cdd:pfam03154  425 PPPPAQP----------PVLTQSQSLPPPAASHPPTSGLHQV----------PSQSPFPQHPFVPGGP--PPITPPSGPP 482

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2120 PAVNesfahPSRAFSQPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSGTARsntDPYSQPP----GTPRPTTVDPYSQQP 2195
Cdd:pfam03154  483 TSTS-----SAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAE---EPESPPPpprsPSPEPTVVNTPSHAS 554

                          330       340       350
                   ....*....|....*....|....*....|
gi 578814480  2196 QTPR----------PSTQTDLFVTPVTNQR 2215
Cdd:pfam03154  555 QSARfykhldrgynSCARTDLYFMPLAGSK 584

ePHD2_PHF6

cd15711

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

4450-4546

1.57e-05

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: 47.39 E-value: 1.57e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHE-EGDGLTDGPARLLNLDlDLWVHLNCALWST---EVYETQAGALINVELA-----LRRGLQMKCVFCHKTGATS 4520
Cdd:cd15711     1 CGFCHAgEEENETRGKLHIFNAK-KAAAHYKCMLFSSgtvQLTTTSRAEFGDFDIKtviqeIKRGKRMKCTLCSQLGATI 79

                          90       100
                  ....*....|....*....|....*.
gi 578814480 4521 GCHRFRCTNIYHFTCAIKAQCMFFKD 4546
Cdd:cd15711    80 GCEIKACVKTYHYHCGVQDKAKYIEN 105

HMG

smart00398

high mobility group;

1669-1722

1.59e-05

high mobility group;

Pssm-ID: 197700 [Multi-domain] Cd Length: 70 Bit Score: 45.77 E-value: 1.59e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 578814480   1669 APVLYTNINFPNLKEEFPDWTT--RVKQIAKLWRKASSQERAPYVQKARDNRAALR 1722
Cdd:smart00398    8 AFMLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63

SET_SETD7

cd10530

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...

4821-4934

1.85e-05

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

Pssm-ID: 380928 Cd Length: 130 Bit Score: 47.29 E-value: 1.85e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4821 VYLARSRIQ--GLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESqnrgvYMFRMDNDHVID------------AT 4886
Cdd:cd10530     9 VYVAESLIPsaGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNG-----NTISLDEETVIDvpepynsvskycAS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480 4887 LtGGPAryiNHSCAPNCVAEVVTFER-GHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd10530    84 L-GHKA---NHSFTPNCIYDPFVHPRfGPIKCIRTLRAVEAGEELTVAY 128

PTZ00449

104 kDa microneme/rhoptry antigen; Provisional

1989-2335

1.88e-05

104 kDa microneme/rhoptry antigen; Provisional

Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 51.23 E-value: 1.88e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1989 PVMTDQFPKSLGLSRSPVVSEQTAKGPIAAGTSDHFTKPSPRADVFQRQRIPDSYARPLLTPAPldsGPGPFKTPMQPPP 2068
Cdd:PTZ00449  498 PIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKP---GPAKEHKPSKIPT 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2069 SSQDPYGSVSQASRRlsvDPyERPALTPRPIDNfshnqsndpySQPPLTPHPAVNESFahpsrafSQPGTISRPTSQDPY 2148
Cdd:PTZ00449  575 LSKKPEFPKDPKHPK---DP-EEPKKPKRPRSA----------QRPTRPKSPKLPELL-------DIPKSPKRPESPKSP 633

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2149 SQPPGTPRPVVDSYSQSSGTARSNTDPYS-QPPGTP--RPTTVDPYSQQPQTPRpSTQTDLFVTPVTNQRHSDPYAHPPG 2225
Cdd:PTZ00449  634 KRPPPPQRPSSPERPEGPKIIKSPKPPKSpKPPFDPkfKEKFYDDYLDAAAKSK-ETKTTVVLDESFESILKETLPETPG 712

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2226 TPrpgISVPYSQPPATPRpriSEGFTRSSMTRPVlMPNQDP------------FLQ--AAQNRGPALPGPLVRPPDTCSQ 2291
Cdd:PTZ00449  713 TP---FTTPRPLPPKLPR---DEEFPFEPIGDPD-AEQPDDiefftppeeertFFHetPADTPLPDILAEEFKEEDIHAE 785

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 2292 TPRPPGPG-LSDTFSRVSPSAARDpYDQSPMTpRSQSDSFGTSQT 2335
Cdd:PTZ00449  786 TGEPDEAMkRPDSPSEHEDKPPGD-HPSLPKK-RHRLDGLALSTT 828

PHD_PRHA_like

cd15504

PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...

1010-1055

1.92e-05

PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and similar proteins; PRHA is a homeodomain protein encoded by a single-copy Arabidopsis thaliana homeobox gene, prha. It shows the capacity to bind to TAATTG core sequence elements but requires additional adjacent bases for high-affinity binding. PRHA contains a plant homeodomain (PHD) finger, a homeodomain, peptide repeats and a putative leucine zipper dimerization domain.

Pssm-ID: 276979 Cd Length: 53 Bit Score: 44.73 E-value: 1.92e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578814480 1010 VCEACGKAT-DPGR-LLLCD-DCDISYHTYCLDPPLQT--VPKG--GWKCKWC 1055
Cdd:cd15504     1 FCAKCQSGEaSPDNdILLCDgGCNRAYHQKCLEPPLLTedIPPEdeGWLCPLC 53

PHD1_Snt2p_like

cd15497

PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...

1011-1055

1.96e-05

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

Pssm-ID: 276972 Cd Length: 48 Bit Score: 44.61 E-value: 1.96e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480 1011 CEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGG--WKCKWC 1055
Cdd:cd15497     2 CKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPNRGfvWSCAPC 48

PHD1_MOZ_d4

cd15526

PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 ...

974-1008

2.24e-05

PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 gene family proteins; MOZ is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity and to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF) is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphoma genesis and bone development, and its homologs. This family also includes three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes via changing the condensed/decondensed state of chromatin in nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro specific gene clusters. All family members contain two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277001 Cd Length: 56 Bit Score: 44.65 E-value: 2.24e-05

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 578814480  974 RLLACSQCGQCYHPYCV--SIKITKVVLSKGWRCLEC 1008
Cdd:cd15526    20 ELISCADCGSSGHPSCLkfSPGLTDAVKSYRWQCIEC 56

PHD2_PHF12_Rco1

cd15534

PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...

391-435

2.31e-05

Pssm-ID: 277009 Cd Length: 47 Bit Score: 44.26 E-value: 2.31e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  391 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNG-WKCKN 435
Cdd:cd15534     1 VCFKCNRSCRVAPLIQCDYCPLLFHLDCLDPPLTHPPATGrWMCPN 46

PHD_Phf1p_Phf2p_like

cd15502

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

1008-1055

3.03e-05

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

Pssm-ID: 276977 Cd Length: 52 Bit Score: 44.35 E-value: 3.03e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578814480 1008 CTVCEaCGKATDPGRLLLCDDCDISYHTYCLDPPLQT----VPKGGWKCKWC 1055
Cdd:cd15502     2 CIVCQ-RGHSPKSNRIVFCDGCNTPYHQLCHDPSIDDevveDPDAEWFCKKC 52

PHD_TIF1_like

cd15541

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

388-436

3.20e-05

Pssm-ID: 277016 [Multi-domain] Cd Length: 43 Bit Score: 43.87 E-value: 3.20e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  388 ECKVCQNckqsGEDSkmLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15541     1 WCAVCQN----GGEL--LCCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC 43

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

3193-3289

3.36e-05

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 3.36e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  3193 QRKQ--YEEWLQETQQLLQMQQKYLEEQigahrksKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQIRK 3270
Cdd:pfam13868   87 QKRQeeYEEKLQEREQMDEIVERIQEED-------QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159

                           90
                   ....*....|....*....
gi 578814480  3271 QQKEHAELIEDYRIKQQQQ 3289
Cdd:pfam13868  160 YLKEKAEREEEREAEREEI 178

PRK07764

DNA polymerase III subunits gamma and tau; Validated

2068-2496

3.51e-05

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 50.37 E-value: 3.51e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2068 PSSQDPYGSVSQA----SRRLSVDPYERPALTPRPidnfshnqsndpySQPPLTPHPAVNEsfAHPSRAFSQPgtISRPT 2143
Cdd:PRK07764  365 PSASDDERGLLARlerlERRLGVAGGAGAPAAAAP-------------SAAAAAPAAAPAP--AAAAPAAAAA--PAPAA 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2144 SQDPYSQPPGTPRPVVDSYSQSSGTARSnTDPYSQPPGTPRPTTVDPYSQQPQtPRPSTQTdlfvtpvtnqrHSDPYAHP 2223
Cdd:PRK07764  428 APQPAPAPAPAPAPPSPAGNAPAGGAPS-PPPAAAPSAQPAPAPAAAPEPTAA-PAPAPPA-----------APAPAAAP 494

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2224 PGTPRPGISVPySQPPATPR---PRISEGFTRSSMTRPVLMpnqDPFLQAAQNRGPAL-----PGPLVR----------- 2284
Cdd:PRK07764  495 AAPAAPAAPAG-ADDAATLRerwPEILAAVPKRSRKTWAIL---LPEATVLGVRGDTLvlgfsTGGLARrfaspgnaevl 570

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2285 -------------------PPDTCSQTPRPPGPGLSDTFSRVSPSAARDPYDQSPMTPRSQSDSFGTSQTAHDVADQPRP 2345
Cdd:PRK07764  571 vtalaeelggdwqveavvgPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAP 650

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2346 GSEGSFCASSNSPMHSQGQQFSGVSQLP---GPVPTSGVTDTQNTVNMAQADTEKLRQRQKLREIILQQQQQKKIAGRQE 2422
Cdd:PRK07764  651 EHHPKHVAVPDASDGGDGWPAKAGGAAPaapPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASA 730

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578814480 2423 KGSQDSPAVPHPGplqhwQPENVNQAFTRPPPPYPGNIRSPVAPPLGPRYAVFPKDQRGPYPPDVASMGMRPHG 2496
Cdd:PRK07764  731 PSPAADDPVPLPP-----EPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRR 799

PHD2_KMT2A_like

cd15507

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

1008-1055

3.53e-05

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

Pssm-ID: 276982 Cd Length: 50 Bit Score: 44.00 E-value: 3.53e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1008 CTVCEACGKATDPgrLLLCDDCDISYHTYCLDPPLQTVP---KGGWKCKWC 1055
Cdd:cd15507     2 CHVCGRKGQAQKQ--LLECEKCQRGYHVDCLGPSYPTKPtrkKKTWICSKC 50

PHD1_MTF2_PHF19_like

cd15499

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...

389-436

3.69e-05

Pssm-ID: 276974 Cd Length: 53 Bit Score: 44.03 E-value: 3.69e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  389 CKVCQNcKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNG---WKCKNC 436
Cdd:cd15499     2 CSICGG-AEARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGdekWFCSRC 51

PHD3_KMT2A

cd15592

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

1088-1137

3.83e-05

Pssm-ID: 277067 Cd Length: 57 Bit Score: 44.21 E-value: 3.83e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578814480 1088 CPVCYRNYREEDL---ILQCRQCDRWMHAVCQNLNTE--EEVENVAD-IGFDCSMC 1137
Cdd:cd15592     2 CPLCDKCYDDDDYeskMMQCGKCDRWVHSKCENLSDEmyEILSNLPEsVAYTCINC 57

ePHD_JMJD2

cd15675

Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...

4450-4543

4.18e-05

Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2 proteins. JMJD2 proteins, also termed lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain. JMJD2D is not included in this family, since it lacks both PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth.

Pssm-ID: 277145 [Multi-domain] Cd Length: 112 Bit Score: 45.81 E-value: 4.18e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGL---TDGparllnldldLWVHLNCALWSTEVY--ETQAGALINVELALRRGLQMKCVFCHK-------TG 4517
Cdd:cd15675     1 CCLCCLRGGALkptTDG----------RWAHVVCAIAIPEVRfsNVPERGPIDISKIPPARLKLKCIYCSKitksmshMG 70

                          90       100
                  ....*....|....*....|....*.
gi 578814480 4518 ATSGCHRFRCTNIYHFTCAIKAQCMF 4543
Cdd:cd15675    71 ACIQCSTGKCTTSFHVTCAHAAGVQM 96

PHD_Phf1p_Phf2p_like

cd15502

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

389-436

4.27e-05

Pssm-ID: 276977 Cd Length: 52 Bit Score: 43.96 E-value: 4.27e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  389 CKVCQnCKQSGEDSKMLVCDTCDKGYHTFCLQPVMK----SVPTNGWKCKNC 436
Cdd:cd15502     2 CIVCQ-RGHSPKSNRIVFCDGCNTPYHQLCHDPSIDdevvEDPDAEWFCKKC 52

PHD

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

1088-1139

4.68e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 43.63 E-value: 4.68e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578814480  1088 CPVCyRNYREEDLILQCRQCDRWMHAVCqnLNTEEEVENVADIGFDCSMCRP 1139
Cdd:pfam00628    2 CAVC-GKSDDGGELVQCDGCDDWFHLAC--LGPPLDPAEIPSGEWLCPECKP 50

ePHD_PHF11

cd15712

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...

252-331

5.07e-05

Pssm-ID: 277182 [Multi-domain] Cd Length: 115 Bit Score: 45.66 E-value: 5.07e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  252 AHHRCVEWSLGVCQMEEPLLVNVD---------KAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAA---GAGTFQ 319
Cdd:cd15712    23 AHQNCLLYSSGFVESEEYNPLNLDrrfdvesvlNEIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALcddAAIETD 102

                          90
                  ....*....|...
gi 578814480  320 DFSHIF-LLCPEH 331
Cdd:cd15712   103 EVRGIYrVFCQKH 115

PHA03247

large tegument protein UL36; Provisional

1873-2167

5.32e-05

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 5.32e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1873 PPAPSRIPIQDSLSQAQTSQPP-SPQVFSPgssnSRPPSPMDPYAKMVGTPRPppvGHSFSRRNsaapvencTPLSSVSR 1951
Cdd:PHA03247 2810 AVLAPAAALPPAASPAGPLPPPtSAQPTAP----PPPPGPPPPSLPLGGSVAP---GGDVRRRP--------PSRSPAAK 2874

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1952 PlqmneTTANRPsPVRDLCSSSTT-NNDPYAKPPDTPRPVMTDQFPKSLGLSRSPVVSEQTAKGP--------IAAGTSD 2022
Cdd:PHA03247 2875 P-----AAPARP-PVRRLARPAVSrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPpppprpqpPLAPTTD 2948

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2023 HFTKPSPRADVFQRQR---IPDSYARP-LLTPAPLDSGPGPfKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPA---LT 2095
Cdd:PHA03247 2949 PAGAGEPSGAVPQPWLgalVPGRVAVPrFRVPQPAPSREAP-ASSTPPLTGHSLSRVSSWASSLALHEETDPPPVslkQT 3027

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2096 PRPIDN----------FSHNQSNDPYSQPPLTPHPavNESFAHPsrafSQPGTISRPTSQDPYSQ---PPGTPRPVVD-S 2161
Cdd:PHA03247 3028 LWPPDDtedsdadslfDSDSERSDLEALDPLPPEP--HDPFAHE----PDPATPEAGARESPSSQfgpPPLSANAALSrR 3101


                  ....*.
gi 578814480 2162 YSQSSG 2167
Cdd:PHA03247 3102 YVRSTG 3107

FimV

COG3170

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];

2141-2471

5.74e-05

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];

Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 49.41 E-value: 5.74e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2141 RPTSQDPYSQPpgTPRPVVDSYSQSSGTARSNTDpYSQPPGTPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRhsDPY 2220
Cdd:COG3170    71 RVTSSRPVNEP--FLDFLVEVNWPSGRLVREYTL-LLDPPAYAAAAAAPAAAPAPAPAAPAAAAAAADQPAAEAA--PAA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2221 AHPPGTPRPGISVPysqPPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPAlpgplvrppdtcSQTPRPPGPgl 2300
Cdd:COG3170   146 SGEYYPVRPGDTLW---SIAARPVRPSSGVSLDQMMVALYRANPDAFIDGNINRLKA------------GAVLRVPAA-- 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2301 sDTFSRVSPSAARDPYdqspmtpRSQSDSFGTSQTAHDVADQPRPGSEgsfcASSNSPMHSQGQQFSGVSQLPGPVPTSG 2380
Cdd:COG3170   209 -EEVAALSPAEARQEV-------QAQSADWAAYRARLAAAVEPAPAAA----APAAPPAAAAAAGPVPAAAEDTLSPEVT 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2381 VTDTQNTVNMAQADTEKLRQR-QKLREIILQQQQQKKIAGRQEKGSQDSPAV-PHPGPLQHWQPENVNQAFTRPPPPYPG 2458
Cdd:COG3170   277 AAAAAEEADALPEAAAELAERlAALEAQLAELQRLLALKNPAPAAAVSAPAAaAAAATVEAAAPAAAAQPAAAAPAPALD 356

                         330
                  ....*....|...
gi 578814480 2459 NirsPVAPPLGPR 2471
Cdd:COG3170   357 N---PLLLAGLLR 366

ePHD_JMJD2B

cd15714

Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...

4450-4539

5.82e-05

Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2B. JMJD2B, also termed lysine-specific demethylase 4B (KDM4B), or JmjC domain-containing histone demethylation protein 3B (JHDM3B), specifically antagonizes the trimethyl group from H3K9 in pericentric heterochromatin and reduces H3K36 methylation in mammalian cells. It plays an essential role in the growth regulation of cancer cells by modulating the G1-S transition and promotes cell-cycle progression through the regulation of cyclin-dependent kinase 6 (CDK6). It interacts with heat shock protein 90 (Hsp90) and its stability can be regulated by Hsp90. JMJD2B also functions as a direct transcriptional target of p53, which induces its expression through promoter binding. Moreover, JMJD2B expression can be controlled by hypoxia-inducible factor 1alpha (HIF1alpha) in colorectal cancer and estrogen receptor alpha (ERalpha) in breast cancer. It is also involved in bladder, lung, and gastric cancer. JMJD2B contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.

Pssm-ID: 277184 Cd Length: 110 Bit Score: 45.31 E-value: 5.82e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGL---TDgparllnldlDLWVHLNCALWSTEVYETQA--GALINVELALRRGLQMKCVFCHKT-----GAT 4519
Cdd:cd15714     1 CCLCNLRGGALqmtTD----------ERWVHVICAIAVPEARFLNVieRHPVDVSAIPEQRWKLKCVYCRKRmkkvsGAC 70

                          90       100
                  ....*....|....*....|
gi 578814480 4520 SGCHRFRCTNIYHFTCAIKA 4539
Cdd:cd15714    71 IQCSYDHCSTSFHVTCAHAA 90

PHD2_PHF14

cd15562

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

345-389

5.84e-05

Pssm-ID: 277037 Cd Length: 50 Bit Score: 43.55 E-value: 5.84e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  345 CAVCDSPGD--LLDQffCTTCGQHYHGMCLDIAVT--PLKRA--GWQCPEC 389
Cdd:cd15562     2 CGICKKSNDqhLLAL--CDTCKLYYHLGCLDPPLTrmPKKTKnsGWQCSEC 50

PTZ00395

Sec24-related protein; Provisional

2055-2205

5.90e-05

Sec24-related protein; Provisional

Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 49.69 E-value: 5.90e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2055 SGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHnqSNDPYSQPP---LTPHPAVNESfAHPSR 2131
Cdd:PTZ00395  415 SNPGNSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPY--SNAPLSNAPpssAKDHHSAYHA-AYQHR 491

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578814480 2132 AFSQPGTiSRPTSQDPYSQPpgtprpvvdsYSQSSGTARSN---TDPY-SQPPGTPRPTTVDPYSQQPQTPRPSTQTD 2205
Cdd:PTZ00395  492 AANQPAA-NLPTANQPAANN----------FHGAAGNSVGNpfaSRPFgSAPYGGNAATTADPNGIAKREDHPEGGTN 558

ePHD_JADE

cd15671

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...

247-316

7.07e-05

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

Pssm-ID: 277141 Cd Length: 112 Bit Score: 45.13 E-value: 7.07e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578814480  247 TGTCWAHHRCVEW----SLGVCQMEEPLlVNVDKAVVSGSTERCAFCK-HLGATIKCCEEKCTQMYHYPCAAGAG 316
Cdd:cd15671    16 SGTKWVHVSCALWipevSIGCPEKMEPI-TKISHIPMSRWALVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQHG 89

PHD3_PHF14

cd15563

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

344-389

7.34e-05

Pssm-ID: 277038 Cd Length: 49 Bit Score: 43.15 E-value: 7.34e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  344 NCAVCDSPGDLLDQFFCTTCGQHYHGMCLD--IAVTPLKRA-GWQCPEC 389
Cdd:cd15563     1 ECCVCKQTGDNSQLVRCDECKLCYHFGCLDppLKKSPKQRGyGWVCEEC 49

SET_KMT2E

cd19182

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

4833-4938

7.35e-05

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

Pssm-ID: 380959 Cd Length: 129 Bit Score: 45.65 E-value: 7.35e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4833 LYAARDIEKHTMVIEYIGTIIRNEV--AN-----RKEK--LYESQNRGVYMfrmdndhVIDATLTGGPARYINHSCAPNC 4903
Cdd:cd19182    21 LKAAKDLPPDTLIIEYRGKFMLREQfeANgyffkRPYPfvLFYSKFHGLEM-------CVDARTFGNEARFIRRSCTPNA 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578814480 4904 VAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDF 4938
Cdd:cd19182    94 EVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFDY 128

PHD3_KMT2B

cd15593

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

468-518

7.76e-05

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

Pssm-ID: 277068 Cd Length: 57 Bit Score: 43.30 E-value: 7.76e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578814480  468 CPFCGKCYHP-ELQKDMLHCNMCKRWVHLECDKPTD--HELDTQLKEE--YICMYC 518
Cdd:cd15593     2 CPICLKCYEDnDYESKMMQCAKCDHWVHAKCEGLSDelYEILSSLPDSvvYSCAPC 57

PHD3_KMT2B

cd15593

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

1088-1121

8.65e-05

Pssm-ID: 277068 Cd Length: 57 Bit Score: 43.30 E-value: 8.65e-05

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 578814480 1088 CPVCYRNYREEDL---ILQCRQCDRWMHAVCQNLNTE 1121
Cdd:cd15593     2 CPICLKCYEDNDYeskMMQCAKCDHWVHAKCEGLSDE 38

PRK07003

DNA polymerase III subunit gamma/tau;

1899-2152

8.73e-05

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 49.08 E-value: 8.73e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1899 FSP----GSSNSRPPSPMDPYAKMVGTPRPPPVGHSFSRRN----SAAPVENCTPLSSVSRPLQMNETTANRPSPVRDLC 1970
Cdd:PRK07003  358 FEPavtgGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAvtavTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATAD 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1971 SSSTTNNDPYAKPPDTPRPVMTDQFPKSLGlsRSPVVSEQTAKGPIAAGTSDHFTKPSPRADVFQRQRIPDSYARPLLTP 2050
Cdd:PRK07003  438 RGDDAADGDAPVPAKANARASADSRCDERD--AQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAA 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2051 APLDSGPGPfktPMQPPPSSQDPYGSVSQASRR-----------------LSVDPYERPALTPRPidnfshnQSNDPYSQ 2113
Cdd:PRK07003  516 ASREDAPAA---AAPPAPEARPPTPAAAAPAARaggaaaaldvlrnagmrVSSDRGARAAAAAKP-------AAAPAAAP 585

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578814480 2114 PPLTPHPAVN----ESFAHPSRAFSQPGTISRPTSQDPYSQPP 2152
Cdd:PRK07003  586 KPAAPRVAVQvptpRARAATGDAPPNGAARAEQAAESRGAPPP 628

PHD6_KMT2C_like

cd15514

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in ...

468-518

8.92e-05

Pssm-ID: 276989 Cd Length: 51 Bit Score: 43.04 E-value: 8.92e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578814480  468 CPFCGKCYHPElqkDML-HCNMCKRWVHLECDK-PTDHELDTQLKEEYICMYC 518
Cdd:cd15514     2 CPVCSRSYNEG---ELIiQCSQCERWLHGACDSlRTEEEAERAADNGYRCLLC 51

ePHD_JMJD2A

cd15713

Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...

4450-4546

9.87e-05

Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2A. JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.

Pssm-ID: 277183 Cd Length: 110 Bit Score: 44.58 E-value: 9.87e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGparllnlDLDLWVHLNCALWSTEVYETQAGALINVELA---LRRgLQMKCVFCHK-----TGATSG 4521
Cdd:cd15713     1 CCLCSLRGGALQRA-------NDDKWVHVMCAVAVLEARFVNIAERSPVDVSkipLQR-FKLKCIFCKKrrkrtAGCCVQ 72

                          90       100
                  ....*....|....*....|....*
gi 578814480 4522 CHRFRCTNIYHFTCAIKAQCMFFKD 4546
Cdd:cd15713    73 CSHGRCPTSFHASCAQAAGVMMQPD 97

HMG-box_BHMG1

cd21977

high mobility group (HMG)-box found in basic helix-loop-helix and HMG box domain-containing ...

1671-1725

1.03e-04

high mobility group (HMG)-box found in basic helix-loop-helix and HMG box domain-containing protein 1 (BHMG1) and similar proteins; BHMG1 is an uncharacterized HMG-box containing protein that contains a degenerate basic motif not likely to bind DNA.

Pssm-ID: 438793 [Multi-domain] Cd Length: 66 Bit Score: 43.07 E-value: 1.03e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578814480 1671 VLYTNINFPNLKEEFPDWTTRV--KQIAKLWRKASSQERAPYVQKARD-NRAALRINK 1725
Cdd:cd21977     9 IMFCRLNRKNYIDKHPGLASTEltKELGQLWRELSAEEKKPYCVRARElSQLHNRKVK 66

PTZ00395

Sec24-related protein; Provisional

2106-2342

1.25e-04

Sec24-related protein; Provisional

Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 48.92 E-value: 1.25e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2106 QSNDPYSQppltphpAVNESFAHPSRAFSQPGTISRPTSQDPYSQPPGTPRPvvdsysqssgtaRSNTdPYSQPPGTPRP 2185
Cdd:PTZ00395  384 HSNASYNC-------AAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAP------------NSNT-PYNNPPNSNTP 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2186 TTVDPYSQQPQTPRPSTQTDLFVTPVTNQRHSDPYAHPP---------GTPRPGISVPYS-QPPATPrpriSEGFTRSSM 2255
Cdd:PTZ00395  444 YSNPPNSNPPYSNLPYSNTPYSNAPLSNAPPSSAKDHHSayhaayqhrAANQPAANLPTAnQPAANN----FHGAAGNSV 519

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2256 TRPVLmpnQDPFLQAAQNRGPALPGplvrPPDTCSQTPRPPGPGLSdtfsrvspsaaRDPYDQSPMTPRSQSDSFGTSQT 2335
Cdd:PTZ00395  520 GNPFA---SRPFGSAPYGGNAATTA----DPNGIAKREDHPEGGTN-----------RQKYEQSDEESVESSSSENSSEN 581


                  ....*..
gi 578814480 2336 AHDVADQ 2342
Cdd:PTZ00395  582 ENEVTDK 588

PHD_TIF1beta

cd15623

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

1011-1055

1.28e-04

PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also termed Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), or KRAB-interacting protein 1 (KRIP-1), or nuclear co-repressor KAP-1, or RING finger protein 96, or tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, acts as a nuclear co-repressor that plays a role in transcription and in DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. In addition, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. TIF1-beta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), which can interact with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and mediates homo- and heterodimerization, a plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region, which interact with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity.

Pssm-ID: 277093 Cd Length: 43 Bit Score: 42.10 E-value: 1.28e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKatdPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 1055
Cdd:cd15623     2 CRVCQK---AGALVMCDQCEFCFHLDCHLPALQEVPGEDWKCLLC 43

PHD1_KMT2A_like

cd15506

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

391-436

1.44e-04

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

Pssm-ID: 276981 Cd Length: 47 Bit Score: 42.35 E-value: 1.44e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480  391 VCQNCKQSGEDsKMLVCDTCDKGYHTFCLQPVMKSVPTNG--WKCKNC 436
Cdd:cd15506     1 LCFLCGSAGLN-ELLYCSVCCEPYHTFCLEEAERPLNINKdnWCCRRC 47

SET_SMYD4

cd10536

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

4895-4951

1.53e-04

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

Pssm-ID: 380934 [Multi-domain] Cd Length: 218 Bit Score: 46.52 E-value: 1.53e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578814480 4895 INHSCAPNCvaeVVTFErGHKIIISSSRRIQKGEEL--CYDYKF---DFED------DQHKIPCHCGA 4951
Cdd:cd10536   154 LNHSCDPNT---IRSFY-GNTIVVRATRPIKKGEEItiCYGPHFsrmKRSErqrllkEQYFFDCSCEA 217

PHD1_Snt2p_like

cd15497

PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...

392-436

1.68e-04

Pssm-ID: 276972 Cd Length: 48 Bit Score: 41.91 E-value: 1.68e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNG--WKCKNC 436
Cdd:cd15497     2 CKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPNRGfvWSCAPC 48

PHD1_BPTF

cd15559

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

392-436

1.82e-04

Pssm-ID: 277034 [Multi-domain] Cd Length: 43 Bit Score: 41.63 E-value: 1.82e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEdskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15559     2 CRVCHKLGD---LLCCETCSAVYHLECVDPPLEEVPEEDWQCEVC 43

PHD_PRKCBP1

cd15538

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

972-1008

2.08e-04

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

Pssm-ID: 277013 Cd Length: 41 Bit Score: 41.54 E-value: 2.08e-04

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 578814480  972 EGRLLACSQCGQCYHPYCVSIKITkvvLSKGWRCLEC 1008
Cdd:cd15538     8 EGQVLCCSLCPRVYHKKCLKLTSE---PDEDWVCPEC 41

ePHD_JADE

cd15671

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...

4475-4538

2.16e-04

Pssm-ID: 277141 Cd Length: 112 Bit Score: 43.59 E-value: 2.16e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578814480 4475 WVHLNCALWSTEV-------YEtqagALINVELALRRGLQMKCVFCH-KTGATSGCHRFRCTNIYHFTCAIK 4538
Cdd:cd15671    20 WVHVSCALWIPEVsigcpekME----PITKISHIPMSRWALVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQ 87

PHD_PRHA_like

cd15504

PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...

389-436

2.20e-04

Pssm-ID: 276979 Cd Length: 53 Bit Score: 42.04 E-value: 2.20e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578814480  389 CKVCQNcKQSGEDSKMLVCD-TCDKGYHTFCLQPVMKSV----PTNGWKCKNC 436
Cdd:cd15504     2 CAKCQS-GEASPDNDILLCDgGCNRAYHQKCLEPPLLTEdippEDEGWLCPLC 53

PHD_UHRF2

cd15617

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...

392-436

2.41e-04

Pssm-ID: 277089 Cd Length: 47 Bit Score: 41.48 E-value: 2.41e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  392 CQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTN-GWKCKNC 436
Cdd:cd15617     2 CYVCGGKQDAHMQLLCDECNMAYHIYCLNPPLDKIPEDeDWYCPSC 47

PRK07764

DNA polymerase III subunits gamma and tau; Validated

2114-2325

2.60e-04

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 2.60e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2114 PPLTPHPAVNESFAHPSRAfsqpgtisRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQ 2193
Cdd:PRK07764  609 PEEAARPAAPAAPAAPAAP--------APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2194 QPQTPRPSTQTdlfvtPVTNQRHSDPYAHPPGTPRPGISV-PYSQPPATPRPRiSEGFTRSSMTRPvLMPNQDPFLQAAQ 2272
Cdd:PRK07764  681 PPPAPAPAAPA-----APAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGA-SAPSPAADDPVP-LPPEPDDPPDPAG 753

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578814480 2273 NRGPALPGPLVRPPDTCSQTPRPPGPGLSDtfsrvsPSAARDPYDQSPMTPRS 2325
Cdd:PRK07764  754 APAQPPPPPAPAPAAAPAAAPPPSPPSEEE------EMAEDDAPSMDDEDRRD 800

PHA03378

EBNA-3B; Provisional

2237-2637

2.77e-04

EBNA-3B; Provisional

Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 47.37 E-value: 2.77e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2237 QPPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRP---PDTCSQTPRPPGPGL-------SDTFSR 2306
Cdd:PHA03378  440 QPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQAPLEPWQPLPHPQVTPvilHQPPAQGVQAHGSMLdllekddEDMEQR 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2307 VSpSAARDPYDQSPMTPRS-----------QSDSFGTSQTAHDvADQPRPGSEGSFCASSNSPMHSQGQQFS-GVSQLPG 2374
Cdd:PHA03378  520 VM-ATLLPPSPPQPRAGRRapcvytedldiESDEPASTEPVHD-QLLPAPGLGPLQIQPLTSPTTSQLASSApSYAQTPW 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2375 PVPTSGVTDTQNTVNMAQADTEKLRQ-RQKLREIILQQQQQKKIAGRQEKG-SQDSPAVPHPGPLQH---------WQPE 2443
Cdd:PHA03378  598 PVPHPSQTPEPPTTQSHIPETSAPRQwPMPLRPIPMRPLRMQPITFNVLVFpTPHQPPQVEITPYKPtwtqighipYQPS 677

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2444 NVNQAFT----------RPPPPYPGNIRSPVAPPLGPRYavfPKDQRGPYPPDVASMG-MRPhgfrfgfPGGSHGTMPSQ 2512
Cdd:PHA03378  678 PTGANTMlpiqwapgtmQPPPRAPTPMRPPAAPPGRAQR---PAAATGRARPPAAAPGrARP-------PAAAPGRARPP 747

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2513 ERF---LVPPQQIQGSGVSPQLRRSVSVDMPRP-LNNSQMNNPVGLPQHF-SPQSLPVQQHNILGQAYIELRHRAPDGRQ 2587
Cdd:PHA03378  748 AAApgrARPPAAAPGRARPPAAAPGAPTPQPPPqAPPAPQQRPRGAPTPQpPPQAGPTSMQLMPRAAPGQQGPTKQILRQ 827

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578814480 2588 RLPFSAPPG--SVVEASSNLRHGNFIPRPDfPGPRHTD-----PMRRPPQGLPNQLP 2637
Cdd:PHA03378  828 LLTGGVKRGrpSLKKPAALERQAAAGPTPS-PGSGTSDkivqaPVFYPPVLQPIQVM 883

PAT1

pfam09770

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...

2135-2371

2.92e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.

Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 47.34 E-value: 2.92e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2135 QPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSNTDPYSQPPGTPRpTTVD---------PYSQQPQTPRPSTQTD 2205
Cdd:pfam09770  106 QPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTGYEKYKEPEPIPD-LQVDaslwgvapkKAAAPAPAPQPAAQPA 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2206 LFVTP---------VTNQ-RhsdpyAHPPGTPRPGISVPYSQPPATPRPRISEGFTRSSMTRPVLMPNQDPfLQAAQNRG 2275
Cdd:pfam09770  185 SLPAPsrkmmsleeVEAAmR-----AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQP-QQPQQHPG 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  2276 PALP-GPLVRPPDTCSQTPRPPGPGLSDTFSRVSPSAA-------RDPYDQSPMTPRSQSDSFGTSQTAHDVADQPRPGS 2347
Cdd:pfam09770  259 QGHPvTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPvqptqilQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGS 338

                          250       260
                   ....*....|....*....|....
gi 578814480  2348 egsfcASSNSPMHSQGQQFSGVSQ 2371
Cdd:pfam09770  339 -----FGRQAPIITHPQQLAQLSE 357

PLN03209

translocon at the inner envelope of chloroplast subunit 62; Provisional

2045-2244

2.96e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional

Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 47.23 E-value: 2.96e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2045 RPLLTPAPLDSGPGPFKTP---MQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSNDPYSQPPLTPHPA 2121
Cdd:PLN03209  381 KPPTSPIPTPPSSSPASSKsvdAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTAPTG 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2122 VNESFAHPSRAFSQPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSgtarsntdpySQPPGTPRPTTVDPYSQQPQTPRPS 2201
Cdd:PLN03209  461 VSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDD----------LKPPTSPSPAAPVGKVAPSSTNEVV 530

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480 2202 TQTDLFV--TPVTNQRHSDPyahppgTPRPgISvPYS-----QPPATPRP 2244
Cdd:PLN03209  531 KVGNSAPptALADEQHHAQP------KPRP-LS-PYTmyedlKPPTSPTP 572

PHD_Int12

cd15501

PHD finger found in integrator complex subunit 12 (Int12) and similar proteins; Int12, also ...

961-1008

2.97e-04

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

Pssm-ID: 276976 Cd Length: 52 Bit Score: 41.56 E-value: 2.97e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  961 CVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLS---KGWRCLEC 1008
Cdd:cd15501     2 CVVCKQMDVTSGNQLVECQECHNLYHQECHKPPVTDKDVNdprLVWYCSRC 52

PHD4_KMT2C

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

345-389

3.24e-04

Pssm-ID: 277071 Cd Length: 57 Bit Score: 41.54 E-value: 3.24e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  345 CAVCDS-----PGDLLDqffCTTCGQHYHGMCLDIAVTP-LKRAGWQCPEC 389
Cdd:cd15596     9 CVVCGSfgqgaEGRLLA---CSQCGQCYHPYCVSIKITKvVLSKGWRCLEC 56

PostSET

smart00508

Cysteine-rich motif following a subset of SET domains;

4943-4959

3.36e-04

Cysteine-rich motif following a subset of SET domains;

Pssm-ID: 214703 Cd Length: 17 Bit Score: 40.47 E-value: 3.36e-04

                            10
                    ....*....|....*..
gi 578814480   4943 HKIPCHCGAVNCRKWMN 4959
Cdd:smart00508    1 KKQPCLCGAPNCRGFLG 17

PHA03377

EBNA-3C; Provisional

1876-2350

3.79e-04

EBNA-3C; Provisional

Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 46.97 E-value: 3.79e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1876 PSRIP----------------IQDSLSQAQTSQPPSP--------QVFSPGSSNSRPP--SPMDPYAKMVGTP--RPPPV 1927
Cdd:PHA03377  496 PSRRRrgacvvydddiievidVETTEEEESVTQPAKPhrkvqdgfQRSGRRQKRATPPkvSPSDRGPPKASPPvmAPPST 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1928 GHSFSRRNSAAPVENCTPLSSvsrPLQMNETTANRPSPV-RDLCSSSTTnndPYAKPPDTPRPVMTDQF--------PKS 1998
Cdd:PHA03377  576 GPRVMATPSTGPRDMAPPSTG---PRQQAKCKDGPPASGpHEKQPPSSA---PRDMAPSVVRMFLRERLleqstgpkPKS 649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1999 LGLSRSPVVSEQTAKGPIA-AGTSDHFTKPSPradvfqrQRIPDSYARPLL---TPAPLDSGPGPFKTPMQPPPSSQDPY 2074
Cdd:PHA03377  650 FWEMRAGRDGSGIQQEPSSrRQPATQSTPPRP-------SWLPSVFVLPSVdagRAQPSEESHLSSMSPTQPISHEEQPR 722

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2075 GSVSQASRRLSVDPYERPalTPRPIDNFSHNQsnDPysQPPLTPHPAVNESF--AHPSRAFSQPGTISRPTSQDPYSQPP 2152
Cdd:PHA03377  723 YEDPDDPLDLSLHPDQAP--PPSHQAPYSGHE--EP--QAQQAPYPGYWEPRppQAPYLGYQEPQAQGVQVSSYPGYAGP 796

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2153 GTPRPVVDSYsqssgtaRSNTDPYSQPPGTPRPTTvdPYSQQPqtPRPSTQTDLFVTPVTNQRHSDPYAHP-PGTPRPGI 2231
Cdd:PHA03377  797 WGLRAQHPRY-------RHSWAYWSQYPGHGHPQG--PWAPRP--PHLPPQWDGSAGHGQDQVSQFPHLQSeTGPPRLQL 865

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2232 S----VPYSQPPAtprprisegftrSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPGPGLsdTFSRV 2307
Cdd:PHA03377  866 SqvpqLPYSQTLV------------SSSAPSWSSPQPRAPIRPIPTRFPPPPMPLQDSMAVGCDSSGTACPSM--PFASD 931

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 2308 SPSAARDPYD---QSPMTPRSQSDSFGTSQTAHDVADQPRPGSEGS 2350
Cdd:PHA03377  932 YSQGAFTPLDinaQTPKRPRVEESSHGPARCSQATTEAQEILSDNS 977

PHD_PHF21A

cd15523

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

345-389

4.60e-04

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 40.84 E-value: 4.60e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  345 CAVCDSPGDLLdqfFCTTCGQHYHGMCLDIAVTPLKRAGWQCPEC 389
Cdd:cd15523     2 CSVCRKSGELL---MCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43

ePHD_ATX1_2_like

cd15662

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...

242-320

5.51e-04

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 are sister paralogs originating from a segmental chromosomal duplication; they are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1 (also known as protein SET domain group 27, or trithorax-homolog protein 1/TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2 (also known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain.

Pssm-ID: 277132 Cd Length: 115 Bit Score: 42.85 E-value: 5.51e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  242 ALFDSTGTCWAHHRCVEW-----SLGVCQMEeplLVNVDKAVvsgSTER----CAFCKH-LGATIKCCEEKCTQMYHYPC 311
Cdd:cd15662    10 ALKPTTDGRWAHLACAIWipetcLLDVKTME---PVDGINAI---SKERwelsCTICKQrYGACIQCSNNSCRVAYHPLC 83


                  ....*....
gi 578814480  312 AAGAGTFQD 320
Cdd:cd15662    84 ARAAGLCME 92

PRK07764

DNA polymerase III subunits gamma and tau; Validated

2129-2359

5.51e-04

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.52 E-value: 5.51e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2129 PSRAFSQPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPysQQPQTPRPSTQTDLFV 2208
Cdd:PRK07764  593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHP--KHVAVPDASDGGDGWP 670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2209 TPVTNQRHSDPYAHPPGTPRPGisvPYSQPPATPRPRisegftrsSMTRPVLMPNQDPFLQAAQNRGPALPgplvRPPDT 2288
Cdd:PRK07764  671 AKAGGAAPAAPPPAPAPAAPAA---PAGAAPAQPAPA--------PAATPPAGQADDPAAQPPQAAQGASA----PSPAA 735

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578814480 2289 CSQTPRPPGPGLSDTFSRVSPSAARDPYDQSPMTPRSQSDSFGTSQTAHDVADQPRPGSEGSFCASSNSPM 2359
Cdd:PRK07764  736 DDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAM 806

PHD4_KMT2C_like

cd15512

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD domain 3 found in ...

389-436

5.62e-04

Pssm-ID: 276987 Cd Length: 49 Bit Score: 40.52 E-value: 5.62e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  389 CKVCQNCKQsGEDSKMLVCDTCDKGYHTFCLQ-PVMKSVPTNGWKCKNC 436
Cdd:cd15512     2 CVSCGSFGR-GAEGRLIACSQCGQCYHPYCVNvKVTKVILSKGWRCLDC 49

ePHD1_PHF6

cd15710

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

241-312

5.79e-04

Pssm-ID: 277180 Cd Length: 115 Bit Score: 42.64 E-value: 5.79e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480  241 QALFDSTGTCWAHHRCVEWSLGVCQME---EPL----LVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 312
Cdd:cd15710    14 QLLISENQKVAAHHKCMLFSSALVSSHsdsENLggfsIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCA 92

PHD5_NSD3

cd15661

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

1011-1054

5.85e-04

PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.

Pssm-ID: 277131 Cd Length: 43 Bit Score: 40.34 E-value: 5.85e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480 1011 CEACGkatDPGRLLLCD--DCDISYHTYCLDppLQTVPKGGWKCKW 1054
Cdd:cd15661     2 CFQCG---DGGELVMCDkkDCPKAYHLLCLN--LTQPPYGKWECPW 42

PHD1_KMT2A_like

cd15506

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

960-1008

6.16e-04

Pssm-ID: 276981 Cd Length: 47 Bit Score: 40.42 E-value: 6.16e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480  960 MCVVCGSFGQGaegRLLACSQCGQCYHPYCVSIKITKVVLSKG-WRCLEC 1008
Cdd:cd15506     1 LCFLCGSAGLN---ELLYCSVCCEPYHTFCLEEAERPLNINKDnWCCRRC 47

SET_SMYD3

cd19203

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...

4896-4934

6.17e-04

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.

Pssm-ID: 380980 [Multi-domain] Cd Length: 210 Bit Score: 44.66 E-value: 6.17e-04

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 578814480 4896 NHSCAPNCVAevvTFErGHKIIISSSRRIQKGEELCYDY 4934
Cdd:cd19203   147 NHSCDPNCVI---VFN-GPHLLLRAIREIEVGEELTISY 181

COG5141

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

4444-4558

6.46e-04

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

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 46.13 E-value: 6.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4444 PKDYRKCCFCHEEgDGLtdgparLLNLDLDLWVHLNCALWSTEVY--ETQAGALINVELALRRGL-QMKCVFCHKTGATS 4520
Cdd:COG5141   244 EYQIRCCSFCPSS-DGA------FKQTSDGRWGHVICAMFNPELSfgHLLSKDPIDNIASVSSSRwKLGCLICKEFGGTC 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480 4521 -GCHRFRCTNIYHFTCAIKAqCMFFK------------DKTMLCPMHKPKG 4558
Cdd:COG5141   317 iQCSYFNCTRAYHVTCARRA-GYFDLniyshngisyciDHEPLCRKHYPLG 366

PHD2_KAT6A_6B

cd15527

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

345-389

6.48e-04

Pssm-ID: 277002 Cd Length: 46 Bit Score: 40.44 E-value: 6.48e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  345 CAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAVTPLKRAGWQCPEC 389
Cdd:cd15527     2 CSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46

ePHD_JMJD2C

cd15715

Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant ...

4450-4536

7.22e-04

Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2C. JMJD2C, also termed lysine-specific demethylase 4C (KDM4C), or gene amplified in squamous cell carcinoma 1 protein (GASC-1 protein), or JmjC domain-containing histone demethylation protein 3C (JHDM3C), is an epigenetic factor that catalyzes the demethylation of di- and trimethylated H3K9 and H3K36, and may be involved in the development and/or progression of various types of cancer including esophageal squamous cell carcinoma (ESC) and breast cancer. It selectively interacts with hypoxia-inducible factor 1alpha (HIF1alpha) and plays a role in breast cancer progression. Moreover, JMJD2C may play an important role in the treatment of obesity and its complications by modulating the regulation of adipogenesis by nuclear receptor peroxisome proliferator-activated receptor gamma (PPARgamma). JMJD2C contains jmjN and jmjC domains in the N-terminal region, followed by a canonical plant homeodomain (PHD) finger, this non-canonical ePHD finger, and a Tudor domain.

Pssm-ID: 277185 Cd Length: 110 Bit Score: 42.25 E-value: 7.22e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 4450 CCFCHEEGDGLTDGPArllnldlDLWVHLNCALWSTEVYETQAGALINVELA---LRRgLQMKCVFCHK-----TGATSG 4521
Cdd:cd15715     1 CCLCNLRGGALKQTSD-------DKWAHVMCAVALPEVRFINVVERTPIDISripLQR-LKLKCIFCRNrikrvSGACIQ 72

                          90
                  ....*....|....*
gi 578814480 4522 CHRFRCTNIYHFTCA 4536
Cdd:cd15715    73 CSYGRCPASFHVTCA 87

PHD1_PHF10

cd15528

PHD finger 1 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...

960-1008

7.68e-04

PHD finger 1 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277003 Cd Length: 54 Bit Score: 40.47 E-value: 7.68e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578814480  960 MCVVC---GSFGQGAEGRLLACSQCGQCYHPYCVSI--KITKVVLSKGWRCLEC 1008
Cdd:cd15528     1 VCGICekgGKSNKGEPEELIHCSQCGNSGHPSCLEMsdEMVAVIKTYPWQCMEC 54

PHD_BRPF_JADE_like

cd15492

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

1008-1055

8.45e-04

PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; The family includes BRPF proteins, Jade proteins, protein AF-10 and AF-17. BRPF proteins are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. Jade proteins are required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6, to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor that has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is a putative transcription factor that may play a role in multiple signaling pathways. All Jade proteins, AF-10, and AF-17 contain a canonical PHD finger followed by a non-canonical ePHD finger. This model corresponds to the canonical PHD finger.

Pssm-ID: 276967 [Multi-domain] Cd Length: 46 Bit Score: 39.91 E-value: 8.45e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480 1008 CTVCEAcGKATDPGRLLLCDDCDISYHTYCLDppLQTVPKGGWKCKWC 1055
Cdd:cd15492     2 CDVCLD-GESEDDNEIVFCDGCNVAVHQSCYG--IPLIPEGDWFCRKC 46

ePHD2_PHF6

cd15711

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

252-312

9.47e-04

Pssm-ID: 277181 Cd Length: 118 Bit Score: 41.99 E-value: 9.47e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578814480  252 AHHRCVEWSLGVCQMEEPL--------LVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 312
Cdd:cd15711    27 AHYKCMLFSSGTVQLTTTSraefgdfdIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCG 95

dnaA

PRK14086

chromosomal replication initiator protein DnaA;

2187-2377

9.47e-04

chromosomal replication initiator protein DnaA;

Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 45.59 E-value: 9.47e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2187 TVDPYSQQPQTPRPstqtdlfvtpvTNQRHSDP-YAHPPGTPRPGisvpYSQPPATPRPrisEGFTRSSMtrpvlMPNQD 2265
Cdd:PRK14086   87 TVDPSAGEPAPPPP-----------HARRTSEPeLPRPGRRPYEG----YGGPRADDRP---PGLPRQDQ-----LPTAR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2266 PFLQAAQNRGPalPGPLVRPPDTCS-QTPR----PPGPGLSDTFSRVSPSAARDPYDQ---SPMTPRSQSDSFGTSQTAH 2337
Cdd:PRK14086  144 PAYPAYQQRPE--PGAWPRAADDYGwQQQRlgfpPRAPYASPASYAPEQERDREPYDAgrpEYDQRRRDYDHPRPDWDRP 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578814480 2338 DVADQ----PRPGSEGSFCASSNSPMHSQGQQFSGVSQLPGPVP 2377
Cdd:PRK14086  222 RRDRTdrpePPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLA 265

PHD

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

1088-1137

1.03e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 39.89 E-value: 1.03e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 578814480   1088 CPVCYRNYREEDLIlQCRQCDRWMHAVCQNLNTEEEVENVadiGFDCSMC 1137
Cdd:smart00249    2 CSVCGKPDDGGELL-QCDGCDRWYHQTCLGPPLLEEEPDG---KWYCPKC 47

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

3198-3280

1.07e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.07e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  3198 EEWLQETQQLLQmqqkylEEQigahrKSKKALSAKQRT--AKKAG-REFPEEDAEQLKHVTEQQSMVQKQLEQIRKQQKE 3274
Cdd:pfam01576  467 ESQLQDTQELLQ------EET-----RQKLNLSTRLRQleDERNSlQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535


                   ....*.
gi 578814480  3275 HAELIE 3280
Cdd:pfam01576  536 DAGTLE 541

PRK12323

DNA polymerase III subunit gamma/tau;

2065-2315

1.08e-03

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.25 E-value: 1.08e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2065 QPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSNDPYSQPPLTPHPAVNESFAHPSRAFSQPGTISRPTS 2144
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAP 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2145 QdPYSQPPGTPRPvvdsysqssgtarsntdPYSQPPGTPRPTTVDPYSQQPqtPRPSTQTDLFVTPVTNQrhsdpyahPP 2224
Cdd:PRK12323  453 A-PAAAPAAAARP-----------------AAAGPRPVAAAAAAAPARAAP--AAAPAPADDDPPPWEEL--------PP 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2225 GTPRPGisvPYSQPPATPrpriseGFTRSSMTRPVLMPNQDPFLQAAQNRgPALPGPLVRPPDTCSQTPRPP---GPGLS 2301
Cdd:PRK12323  505 EFASPA---PAQPDAAPA------GWVAESIPDPATADPDDAFETLAPAP-AAAPAPRAAAATEPVVAPRPPrasASGLP 574

                         250
                  ....*....|....*
gi 578814480 2302 DTFSRVSPS-AARDP 2315
Cdd:PRK12323  575 DMFDGDWPAlAARLP 589

PHD2_KMT2B

cd15591

PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

961-1008

1.26e-03

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

Pssm-ID: 277066 Cd Length: 50 Bit Score: 39.54 E-value: 1.26e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480  961 CVVCGSFGQGAEgRLLACSQCGQCYHPYCVSIKITKVVLSK--GWRCLEC 1008
Cdd:cd15591     2 CHVCGRKNKESK-PLLECERCRNCYHPACLGPNYPKPANRKkrPWICSAC 50

PHD4_KMT2C

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

389-436

1.31e-03

Pssm-ID: 277071 Cd Length: 57 Bit Score: 40.00 E-value: 1.31e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  389 CKVCQNCKQsGEDSKMLVCDTCDKGYHTFCLQ-PVMKSVPTNGWKCKNC 436
Cdd:cd15596     9 CVVCGSFGQ-GAEGRLLACSQCGQCYHPYCVSiKITKVVLSKGWRCLEC 56

PHD2_KMT2C_like

cd15510

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

961-1008

1.41e-03

Pssm-ID: 276985 Cd Length: 46 Bit Score: 39.34 E-value: 1.41e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480  961 CVVCGSfgQGAEGRLLACSQCGQCYHPYCVSIKITKVVlSKGWRCLEC 1008
Cdd:cd15510     2 CQACRQ--PGDDTKMLVCETCDKGYHTSCLRPVMSSIP-KYGWKCKNC 46

PHD_TIF1beta

cd15623

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

389-436

1.45e-03

Pssm-ID: 277093 Cd Length: 43 Bit Score: 39.40 E-value: 1.45e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578814480  389 CKVCQnckqsgEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15623     2 CRVCQ------KAGALVMCDQCEFCFHLDCHLPALQEVPGEDWKCLLC 43

PHD1_AIRE

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

345-389

1.50e-03

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 39.36 E-value: 1.50e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  345 CAVCDSPGDLLdqfFCTTCGQHYHGMCLDIAVTPLKRAGWQCPEC 389
Cdd:cd15539     2 CAVCGDGGELL---CCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43

PHD5_NSD2

cd15660

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

1014-1054

1.52e-03

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fifth PHD finger.

Pssm-ID: 277130 Cd Length: 43 Bit Score: 39.15 E-value: 1.52e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 578814480 1014 CGKATDPGRLLLCDD--CDISYHTYCLDppLQTVPKGGWKCKW 1054
Cdd:cd15660     2 CFRCGDGGQLVLCDRksCTKAYHLSCLG--LTKRPFGKWECPW 42

ePHD_JMJD2

cd15675

Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...

285-331

1.53e-03

Pssm-ID: 277145 [Multi-domain] Cd Length: 112 Bit Score: 41.19 E-value: 1.53e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578814480  285 RCAFCKHL-------GATIKCCEEKCTQMYHYPCAAGAGT---FQDFSH-IFLLCPEH 331
Cdd:cd15675    55 KCIYCSKItksmshmGACIQCSTGKCTTSFHVTCAHAAGVqmePDDWPYpVYVTCTKH 112

PHA03269

envelope glycoprotein C; Provisional

2110-2229

1.57e-03

envelope glycoprotein C; Provisional

Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 44.72 E-value: 1.57e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2110 PYSQPPLTPHPAVnesfAHPSRAFSQPGTISRPTSQdPYSQPPgtprPVVDSYSQSSgtarSNTDPYSQPPGTPRPTtvd 2189
Cdd:PHA03269   46 PHQAASRAPDPAV----APTSAASRKPDLAQAPTPA-ASEKFD----PAPAPHQAAS----RAPDPAVAPQLAAAPK--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 578814480 2190 PYSQQPQTPRPSTQTDLFVTPV-TNQRHSDPYAHPPGTPRP 2229
Cdd:PHA03269  110 PDAAEAFTSAAQAHEAPADAGTsAASKKPDPAAHTQHSPPP 150

PHD2_NSD

cd15565

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

960-1005

1.69e-03

PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the second PHD finger.

Pssm-ID: 277040 Cd Length: 51 Bit Score: 39.33 E-value: 1.69e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  960 MCVVCGSFGQGAEGrLLACSQ--CGQCYHPYCVS-IKITKVVLSKGWRC 1005
Cdd:cd15565     1 SCFVCKKLGSVGGE-VFKCSVasCGKFYHEECLKkWPLTTISDSKKFRC 48

PRK07764

DNA polymerase III subunits gamma and tau; Validated

2066-2314

1.71e-03

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.98 E-value: 1.71e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2066 PPPSSQDPyGSVSQASRRLSVDPYERPALTPRPIDnfshnqsnDPYSQPPLTPHPAVNESFAHPSRAFSQPGTISRPTSQ 2145
Cdd:PRK07764  590 PAPGAAGG-EGPPAPASSGPPEEAARPAAPAAPAA--------PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVP 660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2146 DPYSQPPGTPRPVVDSYSQSSGTArsnTDPYSQPPGTPRPTTvDPYSQQPQTPRPstqtdlfvtpvtnQRHSDPYAHPPG 2225
Cdd:PRK07764  661 DASDGGDGWPAKAGGAAPAAPPPA---PAPAAPAAPAGAAPA-QPAPAPAATPPA-------------GQADDPAAQPPQ 723

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2226 TPRPGISVPYSQPPATPRPRISEGFTRssmtrPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPGPGLSDTFS 2305
Cdd:PRK07764  724 AAQGASAPSPAADDPVPLPPEPDDPPD-----PAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDR 798


                  ....*....
gi 578814480 2306 RVSPSAARD 2314
Cdd:PRK07764  799 RDAEEVAME 807

PHA03379

EBNA-3A; Provisional

2140-2669

1.82e-03

EBNA-3A; Provisional

Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 44.66 E-value: 1.82e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2140 SRPTSQDPYSQPPGTPRPvvdsysqssgtarsntdpysqPPGTPRPTTVDPYSQQP-----QTPRPSTQTDLFVTPVTNQ 2214
Cdd:PHA03379  401 AREALEKASEPTYGTPRP---------------------PVEKPRPEVPQSLETATshgsaQVPEPPPVHDLEPGPLHDQ 459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2215 RHSDPyahppgtprpgisVPYSQPPATPRPRISEGftrssmtrpvlmpnqdpflqaaqnrgPALPGPLVRPPDTCSQTPR 2294
Cdd:PHA03379  460 HSMAP-------------CPVAQLPPGPLQDLEPG--------------------------DQLPGVVQDGRPACAPVPA 500

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2295 PPGPGLSDTFSRVSPSAARDPydqSPMTPRSQSDSFGTSQT-AHDVADQPRPGSEGSFCASSNSPMHSQGQQFSGVSQLP 2373
Cdd:PHA03379  501 PAGPIVRPWEASLSQVPGVAF---APVMPQPMPVEPVPVPTvALERPVCPAPPLIAMQGPGETSGIVRVRERWRPAPWTP 577

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2374 GPVptsgvtdtQNTVNMAQAD-TEKLRQRQKLREiilqqqqqKKIAGRQEKGSQDSPAVPHPGPLQHWQpenvnQAFTRP 2452
Cdd:PHA03379  578 NPP--------RSPSQMSVRDrLARLRAEAQPYQ--------ASVEVQPPQLTQVSPQQPMEYPLEPEQ-----QMFPGS 636

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2453 PPPYPGNI-RSPVAPPLGPRYAVF----PKDQRGPYPPDVASMGMRPhgfrfgfPGGShgtmpSQERFLvppqqiqgsgv 2527
Cdd:PHA03379  637 PFSQVADVmRAGGVPAMQPQYFDLplqqPISQGAPLAPLRASMGPVP-------PVPA-----TQPQYF----------- 693

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2528 spqlrrsvSVDMPRPLNNSQmNNPVGLPQhfSPQSLPVQQHNILGQAYIELRHRAPDGRQRLPFSAPPGSVVEASSNLRH 2607
Cdd:PHA03379  694 --------DIPLTEPINQGA-SAAHFLPQ--QPMEGPLVPERWMFQGATLSQSVRPGVAQSQYFDLPLTQPINHGAPAAH 762

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578814480 2608 gnFIPRPDFPGPrhtdpmRRPPQGLPNQLPVHPDLEQVPpsqqeqgHSVHSSSMVMRTLNHP 2669
Cdd:PHA03379  763 --FLHQPPMEGP------WVPEQWMFQGAPPSQGTDVVQ-------HQLDALGYVLHVLNHP 809

PHD

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

4510-4554

1.82e-03

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 39.12 E-value: 1.82e-03

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578814480   4510 CVFCHKTGATS---GCHRfrCTNIYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:smart00249    2 CSVCGKPDDGGellQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

PHD2_KMT2A_like

cd15507

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

389-436

1.85e-03

Pssm-ID: 276982 Cd Length: 50 Bit Score: 39.37 E-value: 1.85e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  389 CKVCQNCKQSgeDSKMLVCDTCDKGYHTFCLQPVMKSVPT---NGWKCKNC 436
Cdd:cd15507     2 CHVCGRKGQA--QKQLLECEKCQRGYHVDCLGPSYPTKPTrkkKTWICSKC 50

ePHD_BRPF

cd15670

Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...

4475-4539

1.87e-03

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: 41.17 E-value: 1.87e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578814480 4475 WVHLNCALWSTEVYetqagaLIN-VELALRRGLQ--------MKCVFC-HKTGATSGCHRFRCTNIYHFTCAIKA 4539
Cdd:cd15670    19 WAHVVCALWIPEVS------FANtVFLEPIDGIQnipkarwkLTCYICkKRMGACIQCHKKNCYTAFHVTCAQQA 87

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

3189-3288

2.11e-03

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.11e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  3189 VNDSQRKQYEEWLQETQQLLQMQ---QKYLEEQIGAHRKSKKALsakqrtaKKAGREFPEEDAEQLKHVTEQQSMV-QKQ 3264
Cdd:pfam13868  103 MDEIVERIQEEDQAEAEEKLEKQrqlREEIDEFNEEQAEWKELE-------KEEEREEDERILEYLKEKAEREEEReAER 175

                           90       100
                   ....*....|....*....|....*
gi 578814480  3265 LEQIRKQQKEHAELIED-YRIKQQQ 3288
Cdd:pfam13868  176 EEIEEEKEREIARLRAQqEKAQDEK 200

COG5141

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

1005-1141

2.28e-03

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

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 44.20 E-value: 2.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1005 CLECTVCEACgKATDPGRLLLCDDCDISYHTYCLDppLQTVPKGGWKCKWCVWCRHcgatsaglrcewqnNYTQCAPCAS 1084
Cdd:COG5141   193 DDICTKCTST-HNENSNAIVFCDGCEICVHQSCYG--IQFLPEGFWLCRKCIYGEY--------------QIRCCSFCPS 255

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578814480 1085 lsscpvcyrnyreEDLILQCRQCDRWMHAVC---------QNLNTEEEVENVADIG-----FDCSMCRPYM 1141
Cdd:COG5141   256 -------------SDGAFKQTSDGRWGHVICamfnpelsfGHLLSKDPIDNIASVSssrwkLGCLICKEFG 313

mukB

PRK04863

chromosome partition protein MukB;

3195-3288

2.47e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.47e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 3195 KQYEEWLQETQQLLQMQQKY--LEEQIGAHRKSKKALsakQRTAKKAGREFPEEDA---------EQLKHVTEQQSMVQK 3263
Cdd:PRK04863  503 RRLREQRHLAEQLQQLRMRLseLEQRLRQQQRAERLL---AEFCKRLGKNLDDEDEleqlqeeleARLESLSESVSEARE 579

                          90       100
                  ....*....|....*....|....*
gi 578814480 3264 QLEQIRKQQKEHAELIEDYRIKQQQ 3288
Cdd:PRK04863  580 RRMALRQQLEQLQARIQRLAARAPA 604

HMG-box_HMGB_rpt2

cd21979

second high mobility group (HMG)-box found in the high mobility group protein B (HMGB) family; ...

1678-1714

2.68e-03

second high mobility group (HMG)-box found in the high mobility group protein B (HMGB) family; HMGB proteins are chromatin-associated nuclear proteins that act as architectural factors in nucleoprotein structures, which regulate DNA-dependent processes including transcription. In mammals, four family members are present: HMGB1, HMGB2, HMGB3 and HMGB4. They regulate the expression of a wide range of genes through architectural remodeling of the chromatin structure. HMGB1, also called high mobility group protein 1 (HMG-1), is a prototypical alarmin or damage-associated molecular pattern (DAMP) molecule when released from cells. It plays important roles in the regulation of a wide range of processes, including transcription, replication, DNA repair, and nucleosome formation, in the nucleus. It also plays multiple roles in regulating inflammation and responses to cell and tissue stress. HMGB2, also called high mobility group protein 2 (HMG-2), has been implicated in numerous cellular processes, including proliferation, differentiation, apoptosis, and tumor growth. It acts as a chromatin-associated nonhistone protein involved in transcriptional regulation and nucleic-acid-mediated innate immune responses in mammalian. It binds DNA to stabilize nucleosomes and promote transcription. HMGB3, also called high mobility group protein 2a (HMG-2a), or high mobility group protein 4 (HMG-4), is an X-linked member of HMGB family and functions as a universal sentinel for nucleic acid-mediated innate immune responses. HMGB3 has been implicated in the regulation of cellular proliferation and differentiation, as well as inflammatory response. HMGB4 is expressed by neuronal cells and affects the expression of genes involved in neural differentiation. It is a factor that regulates chromatin and expression of neuronal differentiation markers. The family also includes high mobility group protein B1 pseudogene 1 (HMGB1P1) and nuclear auto-antigen Sp-100. HMGB1P1, also called putative high mobility group protein B1-like 1 (HMGB1L1), or putative high mobility group protein 1-like 1 (HMG-1L1), is an HMG-box containing protein that binds preferentially single-stranded DNA and unwinds double-stranded DNA. Sp-100, also called nuclear dot-associated Sp100 protein, or speckled 100 kDa. It is a tumor suppressor that is a major constituent of the promyelocytic leukemia (PML) bodies, a subnuclear organelle involved in many physiological processes including cell growth, differentiation and apoptosis. Through the regulation of ETS1, Sp-100 may play a role in angiogenesis, controlling endothelial cell motility and invasion. It may also play roles in the regulation of telomeres lengthening, TP53-mediated transcription, FAS-mediated apoptosis, etc. In addition, the family includes Drosophila melanogaster high mobility group protein DSP1 (dDSP1) and similar proteins. dDSP1, also called protein dorsal switch 1, is a Drosophila HMG1 protein that binds preferentially single-stranded DNA and unwinds double-stranded DNA. It converts Dorsal and nuclear factor (NF)-kappa B from transcriptional activators to repressors. Members of the HMGB family contain two HMG-box domains. This model corresponds to the second one.

Pssm-ID: 438795 [Multi-domain] Cd Length: 71 Bit Score: 39.32 E-value: 2.68e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 578814480 1678 FPNLKEEFPDWTtrVKQIAK----LWRKASSQERAPYVQKA 1714
Cdd:cd21979    18 RPKIKGEHPGLS--IGDVAKklgeMWNNTSAKDKQPYEKKA 56

PHD1_MTF2

cd15578

PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also ...

389-436

2.78e-03

PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also termed metal regulatory transcription factor 2, or metal-response element DNA-binding protein M96, or polycomb-like protein 2 (PCL2), complexes with the polycomb repressive complex-2 (PRC2) in embryonic stem cells and regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. It recruits the PRC2 complex to the inactive X chromosome and target loci in embryonic stem cells. Moreover, MTF2 is required for PRC2-mediated Hox cluster repression. It activates the Cdkn2a gene and promotes cellular senescence, thus suppressing the catalytic activity of PRC2 locally. MTF2 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. This model corresponds to the first PHD finger.

Pssm-ID: 277053 Cd Length: 53 Bit Score: 38.91 E-value: 2.78e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  389 CKVCQNcKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSV---PTNGWKCKNC 436
Cdd:cd15578     2 CTVCQD-GSSESPNEIVLCDKCGQGYHQLCHNPKIDSSvldPDVPWLCRQC 51

PHD4_NSD

cd15567

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

1011-1055

2.86e-03

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

Pssm-ID: 277042 [Multi-domain] Cd Length: 41 Bit Score: 38.38 E-value: 2.86e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480 1011 CEACGKAtdpGRLLLCDDCDISYHTYCLDppLQTVPKGGWKCKWC 1055
Cdd:cd15567     2 CFICSEG---GSLICCESCPASFHPECLG--LEPPPEGKFYCEDC 41

PHD1_AIRE

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

960-1008

2.99e-03

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 38.20 E-value: 2.99e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  960 MCVVCGsfgqgAEGRLLACSQCGQCYHPYCVSIKITKVVlSKGWRCLEC 1008
Cdd:cd15539     1 ECAVCG-----DGGELLCCDGCPRAFHLACLVPPLTLIP-SGTWRCSSC 43

ePHD_RNO

cd15707

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...

247-312

3.08e-03

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

Pssm-ID: 277177 [Multi-domain] Cd Length: 113 Bit Score: 40.66 E-value: 3.08e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578814480  247 TGTCWAHHRCVEW----SLGVCQMEEPLlVNVDKAVVSGSTERCAFCKH-LGATIKCCEEKCTQMYHYPCA 312
Cdd:cd15707    16 SGTKWAHVSCALWipevSIGCVEKMEPI-TKISSIPASRWALICVLCRErTGACIQCSVKTCKTAYHVTCG 85

PHD_TIF1delta

cd15625

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

392-437

3.14e-03

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

Pssm-ID: 277095 [Multi-domain] Cd Length: 49 Bit Score: 38.40 E-value: 3.14e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  392 CQNCKQSGEdskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNCR 437
Cdd:cd15625     5 CAVCLNGGE---LLCCDRCPKVFHLSCHVPALLSFPVGEWVCTLCR 47

PHD_SF

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

4510-4554

3.33e-03

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 38.45 E-value: 3.33e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480 4510 CVFCHKTGATSG----CHRfrCTNIYHFTCAIKAQCMFFKDKTMLCPMH 4554
Cdd:cd15489     2 CIVCGKGGDLGGellqCDG--CGKWFHADCLGPPLSSFVPNGKWICPVC 48

PLN03209

translocon at the inner envelope of chloroplast subunit 62; Provisional

1908-2204

3.34e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional

Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 43.76 E-value: 3.34e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1908 PPSPMDPYAKMVGTPRPPPVGHSFSRRNSAAPVENCTPLSSVSrplQMNETTANRPSPVRDLCSSSTTNNDpyAKPPDTP 1987
Cdd:PLN03209  312 PLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPVTPEAPSP---PIEEEPPQPKAVVPRPLSPYTAYED--LKPPTSP 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 1988 RPVmtdqfPKSLGLSRSPVVsEQTAKGpiAAGTSDHFTKPSPRADVFQRQRIPDSYARPLLTPAPLDSgpgpFKTPMQPP 2067
Cdd:PLN03209  387 IPT-----PPSSSPASSKSV-DAVAKP--AEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYED----LKPPTSPS 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 2068 PSSQDPYGSVSQASRRLSVDPYERPALTprpidnFSHNQSNDPYSQPPLTPHPAVnesfahpsrAFSQPGTISRPTSQDP 2147
Cdd:PLN03209  455 PTAPTGVSPSVSSTSSVPAVPDTAPATA------ATDAAAPPPANMRPLSPYAVY---------DDLKPPTSPSPAAPVG 519

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578814480 2148 YSQPPGTPRpVVDSYSQSSGTARSNTDPYSQPpgTPRPttVDPYS-----QQPQTPRPSTQT 2204
Cdd:PLN03209  520 KVAPSSTNE-VVKVGNSAPPTALADEQHHAQP--KPRP--LSPYTmyedlKPPTSPTPSPVL 576

DUF4200

pfam13863

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...

3191-3284

3.38e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.

Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 40.63 E-value: 3.38e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480  3191 DSQRKQYEEW---LQETQQLLQMQQKYLEEQIGAHRKSKKALSAKQRTA-KKAgrefpEEDAEQLKHVTEQQSMVQKQLE 3266
Cdd:pfam13863   16 DAKREEIERLeelLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRAlKKA-----EEETKLKKEKEKEIKKLTAQIE 90

                           90
                   ....*....|....*...
gi 578814480  3267 QIRKQQKEHAELIEDYRI 3284
Cdd:pfam13863   91 ELKSEISKLEEKLEEYKP 108

PHD_TIF1gamma

cd15624

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

389-437

3.94e-03

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

Pssm-ID: 277094 Cd Length: 46 Bit Score: 38.10 E-value: 3.94e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  389 CKVCQNckqsGEDskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNCR 437
Cdd:cd15624     2 CAVCQN----GGD--LLCCEKCPKVFHLTCHVPTLLSFPSGDWICTFCR 44

PHD1_DPF3

cd15692

PHD finger 1 found in D4, zinc and double PHD fingers family 3 (DPF3); DPF3, also termed ...

970-1008

3.98e-03

PHD finger 1 found in D4, zinc and double PHD fingers family 3 (DPF3); DPF3, also termed BRG1-associated factor 45C (BAF45C), or zinc finger protein cer-d4, is encoded by a neuro-specific gene, cer-d4. It functions as a new epigenetic key factor for heart and muscle development and may be involved in the transcription regulation of neuro-specific gene clusters. It interacts with the BAF chromatin remodeling complex and binds methylated and acetylated lysine residues of histone 3 and 4. DPF3 contains a nuclear localization signal in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc-finger and a sequence of negatively charged amino acids in the central region, and a cysteine/histidine-rich region that is composed of two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the first PHD finger.

Pssm-ID: 277162 Cd Length: 57 Bit Score: 38.51 E-value: 3.98e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 578814480  970 GAEGRLLACSQCGQCYHPYCV--SIKITKVVLSKGWRCLEC 1008
Cdd:cd15692    16 GRPEELVSCADCGRSGHPTCLqfTVNMTEAVKTYQWQCIEC 56

PHD_TCF19_like

cd15517

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...

391-436

3.99e-03

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).

Pssm-ID: 276992 [Multi-domain] Cd Length: 49 Bit Score: 38.30 E-value: 3.99e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480  391 VCQNCKQSGEDSKML--VCDTCDKGYHTFC--LQPVMKSVPTNgWKCKNC 436
Cdd:cd15517     1 VCGICNLETAAVDELwvQCDGCDKWFHQFClgLSNERYADEDK-FKCPNC 49

PHD_TIF1_like

cd15541

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

345-389

4.20e-03

Pssm-ID: 277016 [Multi-domain] Cd Length: 43 Bit Score: 38.09 E-value: 4.20e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  345 CAVCDSPGDLLdqfFCTTCGQHYHGMCLDIAVTPLKRAGWQCPEC 389
Cdd:cd15541     2 CAVCQNGGELL---CCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC 43

PHD_BAZ2A_like

cd15545

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

961-1008

4.28e-03

Pssm-ID: 277020 [Multi-domain] Cd Length: 46 Bit Score: 38.06 E-value: 4.28e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578814480  961 CVVCGSFGQgaEGRLLACSQCGQCYHPYCVSIKITKVvlSKG-WRCLEC 1008
Cdd:cd15545     2 CQICRSGDN--EDQLLLCDGCDRGYHTYCFKPKMTNV--PEGdWFCPEC 46

PHD_PHF13

cd15632

PHD finger found in PHD finger protein 13 (PHF13); PHF13, also termed survival time-associated ...

474-519

4.95e-03

PHD finger found in PHD finger protein 13 (PHF13); PHF13, also termed survival time-associated PHD finger protein in ovarian cancer 1 (SPOC1), is a novel plant homeodomain (PHD) finger-containing protein that shows strong expression in spermatogonia and ovarian cancer cells, modulates chromatin structure and mitotic chromosome condensation, and is important for proper cell division. It is also required for spermatogonial stem cell differentiation and sustained spermatogenesis. The overexpression of PHF13 associates with unresectable carcinomas and shorter survival in ovarian cancer.

Pssm-ID: 277102 Cd Length: 47 Bit Score: 38.10 E-value: 4.95e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578814480  474 CYHPELQKDMLHCNMCKRWVHLECDKPTdhelDTQLKEEYICMYCK 519
Cdd:cd15632     6 CMKPFAGRPMIECNECHTWIHLSCAKIR----KSNVPEVYVCQKCR 47

PHD1_CHD_II

cd15531

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

345-389

5.06e-03

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 37.58 E-value: 5.06e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  345 CAVCDSPGDLLdqfFCTTCGQHYHGMCLDIAVTPLKRAGWQCPEC 389
Cdd:cd15531     2 CEVCQQGGEII---LCDTCPRAYHLVCLDPELEKAPEGKWSCPHC 43

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

3192-3289

5.14e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 5.14e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 3192 SQRKQYEEWLQETQQLLQMQQKY---LEEQIGAHRKSKKALSAKQ-RTAKKAGREFPEEDAEQLKHVTEQQSMVQ----- 3262
Cdd:PRK00409  527 ELERELEQKAEEAEALLKEAEKLkeeLEEKKEKLQEEEDKLLEEAeKEAQQAIKEAKKEADEIIKELRQLQKGGYasvka 606

                          90       100
                  ....*....|....*....|....*..
gi 578814480 3263 KQLEQIRKQQKEHAELIEDYRIKQQQQ 3289
Cdd:PRK00409  607 HELIEARKRLNKANEKKEKKKKKQKEK 633

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

3189-3295

5.22e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814480 3189 VNDSQRKQYEEwLQETQQLLQMQQKYLEEQigahRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQI 3268
Cdd:COG4942   144 LAPARREQAEE-LRADLAELAALRAELEAE----RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                          90       100
                  ....*....|....*....|....*..
gi 578814480 3269 RKQQKEHAELIEDYRIKQQQQCAMAPP 3295
Cdd:COG4942   219 QQEAEELEALIARLEAEAAAAAERTPA 245

PHD3_KMT2D

cd15597

PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

345-389

5.29e-03

Pssm-ID: 277072 Cd Length: 51 Bit Score: 38.09 E-value: 5.29e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578814480  345 CAVCDS-----PGDLLDqffCTTCGQHYHGMCLDIAVTPLK-RAGWQCPEC 389
Cdd:cd15597     3 CVVCGSfgrgsEGHLLA---CSQCSQCYHPYCVNSKITKVMlLKGWRCVEC 50

PHD_PHF21B

cd15524

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

392-436

5.43e-03

Pssm-ID: 276999 [Multi-domain] Cd Length: 43 Bit Score: 37.57 E-value: 5.43e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578814480  392 CQNCKQSGEdskMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 436
Cdd:cd15524     2 CAACKRGGN---LQPCGTCPRAYHLDCLDPPLKTAPKGVWVCPKC 43

PHD1_MTF2

cd15578

PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also ...

1008-1056

5.81e-03

Pssm-ID: 277053 Cd Length: 53 Bit Score: 37.76 E-value: 5.81e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578814480 1008 CTVCEAcGKATDPGRLLLCDDCDISYHTYCLDPPLQTV---PKGGWKCKWCV 1056
Cdd:cd15578     2 CTVCQD-GSSESPNEIVLCDKCGQGYHQLCHNPKIDSSvldPDVPWLCRQCV 52

PHD_ash2p_like

cd15583

PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and ...

1090-1141

5.95e-03

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

Pssm-ID: 277058 Cd Length: 50 Bit Score: 37.71 E-value: 5.95e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578814480 1090 VCY----RNYREEDLilQCRQCDRWMHAVCqnlnteeevenvadIGFDCSMCRPYM 1141
Cdd:cd15583     1 YCYcgkdRNLGEVEL--QCSICLKWFHAKC--------------VSIDNGSCLPFM 40

PHD1_Rco1

cd15535

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

960-1008

8.43e-03

Pssm-ID: 277010 [Multi-domain] Cd Length: 45 Bit Score: 37.01 E-value: 8.43e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578814480  960 MCVVCGsfgqgAEGRLLACSQCGQCYHPYCVSIKITKVVLSKG-WRCLEC 1008
Cdd:cd15535     1 FCSACG-----GYGSFLCCDGCPRSFHFSCLDPPLEEDNLPDDeWFCNEC 45

Atrophin-1