SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 4758 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 4837
Cdd:cd19171    1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91718902 4838 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4910
Cdd:cd19171   81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  247 GTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLL 326
Cdd:cd15696    7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86

                 ....
gi 91718902  327 CPEH 330
Cdd:cd15696   87 CPTH 90

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 91718902  952 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 1008
Cdd:cd15596    1 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 57

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 91718902 1009 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1055
Cdd:cd15513    1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 91718902  466 LCPFCGKCYHPELQKDMLHCNMCKRWVHLECDKPTDHELDTQLKEEYICMYC 517
Cdd:cd15511    1 PCPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  1876 PPSPQVFSPGSSNSRPPSPMdpYAkmvgtPRPP-PVGHSFSRRNSAAPvENCTPLSSVSRPLQMNETTANRPSPvrdlcs 1954
Cdd:PHA03247 2553 PPLPPAAPPAAPDRSVPPPR--PA-----PRPSePAVTSRARRPDAPP-QSARPRAPVDDRGDPRGPAPPSPLP------ 2618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  1955 ssttnndPYAKPPDTPRPvmtdqfpkslglSRSPVVSEQTAKGPIAAGTSDHFTK-PSPRAdvFQRQRIPDSYARPlltp 2033
Cdd:PHA03247 2619 -------PDTHAPDPPPP------------SPSPAANEPDPHPPPTVPPPERPRDdPAPGR--VSRPRRARRLGRA---- 2673

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  2034 apldsgPGPFKTPMQP-PPSSQDPYGSVSQASRRLSVDPYERPA------LTPRPIDNFSHNQSNDPYSQPPLTPHPAVN 2106
Cdd:PHA03247 2674 ------AQASSPPQRPrRRAARPTVGSLTSLADPPPPPPTPEPAphalvsATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  2107 ESFAHPSRAFSQPGTISRPTSQDPYSQPPGTP-----RPVVDSYSQSSGTARSNTDPYSQPPGTPRPTTVDPYSQQPQTP 2181
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAGPprrltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP 2827

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  2182 RPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPGISV----PYSQPPATP----RPRIsegftrSSMTRPVLMPNQDPFLQA 2253
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVrrrpPSRSPAAKPaapaRPPV------RRLARPAVSRSTESFALP 2901

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  2254 A-------QNRGPALPGPLVRPPDTCSQTPRPPGPGLSDT--FSRVSPSAARDPYDQSPmTPRSQSDSFGTSQTAHDVAD 2324
Cdd:PHA03247 2902 PdqperppQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPplAPTTDPAGAGEPSGAVP-QPWLGALVPGRVAVPRFRVP 2980

                         490       500
                  ....*....|....*....|....*....
gi 91718902  2325 QPRPGSEGSfcASSNSPMHsqGQQFSGVS 2353
Cdd:PHA03247 2981 QPAPSREAP--ASSTPPLT--GHSLSRVS 3005

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91718902   4551 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 4602
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   3176 QRKQ--YEEWLQETQQLLQMQQKYLEEQigahrksKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQIRK 3253
Cdd:pfam13868   87 QKRQeeYEEKLQEREQMDEIVERIQEED-------QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159

                           90
                   ....*....|....*....
gi 91718902   3254 QQKEHAELIEDYRIKQQQQ 3272
Cdd:pfam13868  160 YLKEKAEREEEREAEREEI 178

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 4758 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 4837
Cdd:cd19171    1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91718902 4838 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4910
Cdd:cd19171   81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902  247 GTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSHIFLL 326
Cdd:cd15696    7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86

                 ....
gi 91718902  327 CPEH 330
Cdd:cd15696   87 CPTH 90

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 4770 KSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRgvYMFRMDNDHVIDATLTGGPARYINH 4849
Cdd:COG2940    5 HPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINH 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 4850 SCAPNCVAEvvtfERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHkiPCHCGavNCRKW 4909
Cdd:COG2940   83 SCDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902    4772 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNR-GVYMFRMDNDHVIDATLTGGPARYINHS 4850
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHS 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 91718902    4851 CAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDD 4893
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 91718902 1009 VCEACGKATDPGRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 1055
Cdd:cd15513    1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 91718902  390 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPVMKSVPTNGWKCKNC 435
Cdd:cd15594    1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902    4610 VFVIRIVEQGheDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPGVEACENYTF 4689
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78

                    ....*...
gi 91718902    4690 RYGRNPLM 4697
Cdd:smart00542   79 RYHRSPLL 86

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 91718902  343 NCAVCDSPGDLLDQFFCTTCGQHYHGMCLDIAV--TPLKRAGWQCPEC 388
Cdd:cd15509    1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91718902   4551 GSLIFHTIGQLLPQQMqAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSI 4602
Cdd:pfam05964    1 GSLTVLSLGEIVPDRP-AFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   4429 HLNCALWSTEVYetQAGA------LINVELALRRGLQMKCVFCH-KTGATSGCHRFRCTNIYHFTCAIKAQCMF-FKDKT 4500
Cdd:pfam13771    1 HVVCALWSPELV--QRGNdsmgfpIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDN 78

                           90
                   ....*....|
gi 91718902   4501 ----MLCPMH 4506
Cdd:pfam13771   79 gtfkSYCKKH 88

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902    252 HHRCVEWSLGVCQ-----MEEPLLvNVDKAVVSGSTERCAFCKH-LGATIKCCEEKCTQMYHYPCAAGAG---TFQDFSH 322
Cdd:pfam13771    1 HVVCALWSPELVQrgndsMGFPIE-DIEKIPKRRWKLKCYLCKKkGGACIQCSKKNCRRAFHVTCALEAGllmQFDEDNG 79

                   ....*....
gi 91718902    323 IFLL-CPEH 330
Cdd:pfam13771   80 TFKSyCKKH 88

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 91718902    390 VCQNCKQSGEDSKMLVCDTCDKGYHTFCLQPV--MKSVPTNGWKCKNCRIC 438
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPldPAEIPSGEWLCPECKPK 51

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2010 PSPRADvfqrQRIPDSYARP--LLTPAPLDSGPGPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDnfsh 2087
Cdd:pfam03154  149 PSPQDN----ESDSDSSAQQqiLQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQ---- 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2088 nqsndpySQPPLTPHPAVNESFA-HPSRAFS-----QPGTISRPTSQDPysqPPGTPRPVVDSYSQSSGTARSNTDPYSQ 2161
Cdd:pfam03154  221 -------TQSTAAPHTLIQQTPTlHPQRLPSphpplQPMTQPPPPSQVS---PQPLPQPSLHGQMPPMPHSLQTGPSHMQ 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2162 PPGTPRPTTVDPYSQQPQTP-RPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPG------ISVPYSQPP-ATPRPRISegf 2233
Cdd:pfam03154  291 HPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQplppapLSMPHIKPPpTTPIPQLP--- 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2234 TRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPGPGLSDTFSRVSPSAARDP-YDQSPMTPRSQSdS 2312
Cdd:pfam03154  368 NPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPvLTQSQSLPPPAA-S 446

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 91718902   2313 FGTSQTAHDVADQPrPGSEGSFCASSNSPMHS-QGQQFSGVSQLPGPVPTSGVT 2365
Cdd:pfam03154  447 HPPTSGLHQVPSQS-PFPQHPFVPGGPPPITPpSGPPTSTSSAMPGIQPPSSAS 499

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.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 91718902     959 MCVVCGSFGqgAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLEC 1007
Cdd:smart00249    1 YCSVCGKPD--DGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

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.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 91718902     467 CPFCGKCYHPElqkDMLHCNMCKRWVHLECDKPTDHELDtqLKEEYICMYC 517
Cdd:smart00249    2 CSVCGKPDDGG---ELLQCDGCDRWYHQTCLGPPLLEEE--PDGKWYCPKC 47

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91718902    467 CPFCGKcyhPELQKDMLHCNMCKRWVHLECDKPTDhELDTQLKEEYICMYCK 518
Cdd:pfam00628    2 CAVCGK---SDDGGELVQCDGCDDWFHLACLGPPL-DPAEIPSGEWLCPECK 49

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2219 SQPPATPRPRISEGFTRSSMTRPVLMpNQDPFLQAAQnrGPALPGPLVRPPDTCSQTPRPPgPGLSDTFSRVSPSAARDP 2298
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQ-TQPPVLQAQS--GAASPPSPPPPGTTQAATAGPT-PSAPSVPPQGSPATSQPP 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2299 YDQSPM---------TPRSQSDSFGTSQTAHDVADQPRPGSEGSFCASSNSPMHSQGQQF-----SGVSQLPGPVPTSGV 2364
Cdd:pfam03154  219 NQTQSTaaphtliqqTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMphslqTGPSHMQHPVPPQPF 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2365 TDTQntvNMAQADTEKLRQRQklreiilqqQQQKKIAGRQEKGSQDSPAVPHPGPLQHWQPENVNQAFTRPPPPYP---- 2440
Cdd:pfam03154  299 PLTP---QSSQSQVPPGPSPA---------APGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPipql 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   2441 GNIRSPVAPPLGPRYAVFPKDQRGPYPPDVASMGMRPHgfrfGFPGGSH----GTMPSQERFLVPPQQIQGSGVSPQLRR 2516
Cdd:pfam03154  367 PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLST----HHPPSAHppplQLMPQSQQLPPPPAQPPVLTQSQSLPP 442

                          330       340       350
                   ....*....|....*....|....*....|..
gi 91718902   2517 SVSvDMPRPLNNSQMNNPVGLPQH-FSPQSLP 2547
Cdd:pfam03154  443 PAA-SHPPTSGLHQVPSQSPFPQHpFVPGGPP 473

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902   3176 QRKQ--YEEWLQETQQLLQMQQKYLEEQigahrksKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQIRK 3253
Cdd:pfam13868   87 QKRQeeYEEKLQEREQMDEIVERIQEED-------QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159

                           90
                   ....*....|....*....
gi 91718902   3254 QQKEHAELIEDYRIKQQQQ 3272
Cdd:pfam13868  160 YLKEKAEREEEREAEREEI 178

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 2124 RPTSQDPYSQPpgTPRPVVDSYSQSSGTARSNTDpYSQPPGTPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRhsDPY 2203
Cdd:COG3170   71 RVTSSRPVNEP--FLDFLVEVNWPSGRLVREYTL-LLDPPAYAAAAAAPAAAPAPAPAAPAAAAAAADQPAAEAA--PAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 2204 AHPPGTPRPGISVPysqPPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPAlpgplvrppdtcSQTPRPPGPgl 2283
Cdd:COG3170  146 SGEYYPVRPGDTLW---SIAARPVRPSSGVSLDQMMVALYRANPDAFIDGNINRLKA------------GAVLRVPAA-- 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 2284 sDTFSRVSPSAARDPYdqspmtpRSQSDSFGTSQTAHDVADQPRPGSEgsfcASSNSPMHSQGQQFSGVSQLPGPVPTSG 2363
Cdd:COG3170  209 -EEVAALSPAEARQEV-------QAQSADWAAYRARLAAAVEPAPAAA----APAAPPAAAAAAGPVPAAAEDTLSPEVT 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 2364 VTDTQNTVNMAQADTEKLRQR-QKLREIILQQQQQKKIAGRQEKGSQDSPAV-PHPGPLQHWQPENVNQAFTRPPPPYPG 2441
Cdd:COG3170  277 AAAAAEEADALPEAAAELAERlAALEAQLAELQRLLALKNPAPAAAVSAPAAaAAAATVEAAAPAAAAQPAAAAPAPALD 356

                        330
                 ....*....|...
gi 91718902 2442 NirsPVAPPLGPR 2454
Cdd:COG3170  357 N---PLLLAGLLR 366

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 4396 PKDYRKCCFCHEEgDGLtdgparLLNLDLDLWVHLNCALWSTEVY--ETQAGALINVELALRRGL-QMKCVFCHKTGATS 4472
Cdd:COG5141  244 EYQIRCCSFCPSS-DGA------FKQTSDGRWGHVICAMFNPELSfgHLLSKDPIDNIASVSSSRwKLGCLICKEFGGTC 316

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 91718902 4473 -GCHRFRCTNIYHFTCAIKAqCMFFK------------DKTMLCPMHKPKG 4510
Cdd:COG5141  317 iQCSYFNCTRAYHVTCARRA-GYFDLniyshngisyciDHEPLCRKHYPLG 366

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.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 91718902    4462 CVFCHKTGATS---GCHRfrCTNIYHFTCAIKAQCMFFKDKTMLCPMH 4506
Cdd:smart00249    2 CSVCGKPDDGGellQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 3172 VNDSQRKQYEEwLQETQQLLQMQQKYLEEQigahRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSMVQKQLEQI 3251
Cdd:COG4942  144 LAPARREQAEE-LRADLAELAALRAELEAE----RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                         90       100
                 ....*....|....*....|....*..
gi 91718902 3252 RKQQKEHAELIEDYRIKQQQQCAMAPP 3278
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAERTPA 245

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 4758 KSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDA 4837
Cdd:cd19171    1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91718902 4838 TLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4910
Cdd:cd19171   81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91718902 4756 HSKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVI 4835
Cdd:cd19209    1 HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91718902 4836 DATLTGGPARYINHSCAPNCVAEVVTFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 4910
Cdd:cd19209   81 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155

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).