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Conserved domains on  [gi|1658251387|ref|XP_029102169|]
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histone-lysine N-methyltransferase 2C isoform X3 [Scleropages formosus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
4846-4998 9.79e-115

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


:

Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 360.98  E-value: 9.79e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4846 KSSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVIDA 4925
Cdd:cd19171      1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4926 TITGGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWM 4998
Cdd:cd19171     81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
4488-4592 2.21e-72

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: 237.64  E-value: 2.21e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15697      1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80
                           90       100
                   ....*....|....*....|....*
gi 1658251387 4568 VYHFTCALKAQCTFFKDKTMLCHAH 4592
Cdd:cd15697     81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
HMG-box_KMT2C cd22026
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...
1663-1743 2.48e-55

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: 188.07  E-value: 2.48e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1663 QRSTLKWEKEETLGEMATVAPVLYTNMNFPNLKEEFPDWSTRVKQIAKLWRKASSQERSPYVQKARDNRAALRINKVQMS 1742
Cdd:cd22026      1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80

                   .
gi 1658251387 1743 N 1743
Cdd:cd22026     81 N 81
PHD_SF super family cl22851
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
247-330 1.62e-44

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.


The actual alignment was detected with superfamily member cd15696:

Pssm-ID: 473978  Cd Length: 90  Bit Score: 157.41  E-value: 1.62e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  247 GQCCAHQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFRKLTLL 326
Cdd:cd15696      7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86

                   ....
gi 1658251387  327 CPKH 330
Cdd:cd15696     87 CPTH 90
PHD_SF super family cl22851
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
937-992 6.16e-35

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.


The actual alignment was detected with superfamily member cd15596:

Pssm-ID: 473978  Cd Length: 57  Bit Score: 128.98  E-value: 6.16e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387  937 FTMRQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLECT 992
Cdd:cd15596      2 FTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 57
PHD5_KMT2C_like cd15513
PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...
993-1039 9.89e-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: 113.73  E-value: 9.89e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCV 1039
Cdd:cd15513      1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47
PHD2_KMT2C cd15594
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
390-435 1.08e-28

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: 110.80  E-value: 1.08e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15594      1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46
PHD_SF super family cl22851
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
1071-1120 1.86e-27

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.


The actual alignment was detected with superfamily member cd15600:

Pssm-ID: 473978  Cd Length: 51  Bit Score: 107.32  E-value: 1.86e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1071 CPICCHDYRQDELIVQCRQCDRWMHACCQNLNSDEEVENVADDGFECAMC 1120
Cdd:cd15600      2 CPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC 51
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
4697-4780 2.24e-25

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: 102.69  E-value: 2.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4697 PEFIIRVVEQgyEDLVLKGTTPKGVWDQVLEQVAQHRTETGTLKLFPVYLKGEDLFGLTVSAVTRIIESLPGVEACENYA 4776
Cdd:pfam05965    2 PLFRVTVEED--PDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYK 79

                   ....
gi 1658251387 4777 FRYG 4780
Cdd:pfam05965   80 FRYG 83
PHD1_KMT2C_like cd15509
PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
343-388 6.26e-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: 97.38  E-value: 6.26e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  343 NCAVCDSPGDLLDQLFCTTCGQHYHGTCLDIGV--TPLKRAGWQCPEC 388
Cdd:cd15509      1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1893-2423 3.22e-20

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 100.40  E-value: 3.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1893 PTSGSLDDVFLRPQPPPPTGTRLTEAcsqgQASQPQSPQMFSTGTASSSSRPSSPWDPYAKMVGTPRPP------PIGSS 1966
Cdd:PHA03247  2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAapdrsvPPPRP 2573
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1967 TPRRNSTESCSAPRLPSEQQERGRPSSGHESFGSP----TSASVDPYAKPPDTPRPAVTADPFVKPMGPPKAGIVLEsQG 2042
Cdd:PHA03247  2574 APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPrgpaPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-RP 2652
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2043 RHMPASvigdAFARPSHRAEAYQRMSHNKMVLSDPySKPLLTPIPGSNESGSVPLFKAPMPPPHPQDLYNSTPSIGRRNS 2122
Cdd:PHA03247  2653 RDDPAP----GRVSRPRRARRLGRAAQASSPPQRP-RRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA 2727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2123 VDSFERPTRLsdtfsqnsqnDPYAHP-PLTPCTSMNDNFSNSPKMMHHPQSNA--FCQPMPMVRHPSRDAFAQASSTSRS 2199
Cdd:PHA03247  2728 ARQASPALPA----------APAPPAvPAGPATPGGPARPARPPTTAGPPAPAppAAPAAGPPRRLTRPAVASLSESRES 2797
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2200 DFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQ--PPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYS 2277
Cdd:PHA03247  2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPtaPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2278 PQQPSNRRSS---PSHAMEPYPQPPGTPCPgtgerfskspvsQRNADSyfqqPETPRlvkndtyaQQPNIPKPVLSDPYS 2354
Cdd:PHA03247  2878 PARPPVRRLArpaVSRSTESFALPPDQPER------------PPQPQA----PPPPQ--------PQPQPPPPPQPQPPP 2933
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 2355 QPPGTPRPGVGPEVFNRPVARTGPVSQDPFSSPQVTMQENFVRPQTPKHsglsddgfAQPQSNPASQTP 2423
Cdd:PHA03247  2934 PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQP--------APSREAPASSTP 2994
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
4639-4690 1.44e-17

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: 79.09  E-value: 1.44e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387 4639 GSLVLHTVGQLLPQQMAaFHGSSAIFPVGYESSRIYWSMRHGNRRCRYLCSI 4690
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPA-FHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
PHD3_KMT2C cd15511
PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
469-519 8.48e-12

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: 62.89  E-value: 8.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  469 CPLCGKPLGAEFLSDHLTCQSCKRYLHLECERQAGGRTDPLDREGYICTLC 519
Cdd:cd15511      2 CPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
2205-2754 6.29e-10

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 66.26  E-value: 6.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2205 SPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQ--------- 2275
Cdd:PRK10263   376 APEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAwqaeeqqst 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2276 YSPQ---QPSNRRSSPSHAMEPYPQPPGTPCPGTGErfsKSPVSQRNADS-----YFQQPETPRLVKNDTYAQ--QPnIP 2345
Cdd:PRK10263   456 FAPQstyQTEQTYQQPAAQEPLYQQPQPVEQQPVVE---PEPVVEETKPArpplyYFEEVEEKRAREREQLAAwyQP-IP 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2346 KPVlSDPYSQPPGTPRPGVGPEVFNRPVARTGPVSQdpfSSPQVTMqenfvrpqtpkHSGlSDDGFAQPQSNPASQTpvh 2425
Cdd:PRK10263   532 EPV-KEPEPIKSSLKAPSVAAVPPVEAAAAVSPLAS---GVKKATL-----------ATG-AAATVAAPVFSLANSG--- 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2426 dpyaqapmTPRPQ----LGDRLAREVKDQVEVGHEGSSHGVG----QFSNLQQSTSNSTESQSGAQLPLGDTEEkLRQRQ 2497
Cdd:PRK10263   593 --------GPRPQvkegIGPQLPRPKRIRVPTRRELASYGIKlpsqRAAEEKAREAQRNQYDSGDQYNDDEIDA-MQQDE 663
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2498 RLRELILRQQQQKSAIRQEKglqepsssipgTPRQWSQEETGQQNELfnrppppypgtARGSVISTGQRFPGLFPGeqrG 2577
Cdd:PRK10263   664 LARQFAQTQQQRYGEQYQHD-----------VPVNAEDADAAAEAEL-----------ARQFAQTQQQRYSGEQPA---G 718
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2578 AfqNEGQFPRAQFSADVANMGMRPPEPRFGfPSGGQVTLGGQGHFLRSPHHMQGPMIDVPQQMRRslsvdlsrtignnsl 2657
Cdd:PRK10263   719 A--NPFSLDDFEFSPMKALLDDGPHEPLFT-PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQ--------------- 780
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2658 llpqhfPPRSIPLQQHniMGQPFIELRHRAPENRVRLPFAPPAiagnvvdqsvQSQRPADPMLSQPsgitSHMQISSSME 2737
Cdd:PRK10263   781 ------PQQPVAPQPQ--YQQPQQPVAPQPQYQQPQQPVAPQP----------QYQQPQQPVAPQP----QYQQPQQPVA 838
                          570       580
                   ....*....|....*....|....
gi 1658251387 2738 NPHQQSL--PL-----NTEPQQAP 2754
Cdd:PRK10263   839 PQPQDTLlhPLlmrngDSRPLHKP 862
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
3355-3633 2.26e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 57.33  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3355 QQPPMVAGMQPQTVMLSGG---PPINQPRMSPMMQMQPYHNQPNAPRMSGIPGWHPGAPRPIGPGVPAPMASQAPSANTV 3431
Cdd:pfam09606  173 QMGPNGGPGQGQAGGMNGGqqgPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQG 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3432 QPVQTANGGGAPHvKFDDNNPFSEGFQERERKERLREQQERQRVQLMQEVERQRALQQRMEMEQQGLLGPDGNQDTLSQM 3511
Cdd:pfam09606  253 QQSQLGMGINQMQ-QMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMN 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3512 AFYG-----TDLPRDFM---QPQRPSAPQQMFPQQGVQPSFMSSSPGTFFMQTGERRPLIGngsfsseMGPSFRPKHLML 3583
Cdd:pfam09606  332 QSVGqggqvVALGGLNHletWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF-------MRQSPQPSVPSP 404
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 3584 QGPSFGPGQPRPPGFT-GPGMMPQGSadgPPFGVESATPLPPNYPGSGQSL 3633
Cdd:pfam09606  405 QGPGSQPPQSHPGGMIpSPALIPSPS---PQMSQQPAQQRTIGQDSPGGSL 452
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
3256-3348 5.89e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.60  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3256 QKKQYEEWLQHTQ-QLLKMQQKFLEEQIGAHR---KSKKALSAKQRTAKKAgREFpEEDAEQLKHVTEQQSVVQKQLE-Q 3330
Cdd:pfam20492    7 EKQELEERLKQYEeETKKAQEELEESEETAEEleeERRQAEEEAERLEQKR-QEA-EEEKERLEESAEMEAEEKEQLEaE 84
                           90
                   ....*....|....*...
gi 1658251387 3331 IRKQQKEHAELIEEYRVK 3348
Cdd:pfam20492   85 LAEAQEEIARLEEEVERK 102
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
3022-3424 1.14e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.38  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3022 VPTDHSGPGAQGSQLAGMPQN-SSLLMAPGHIQEVEMNPSVTIGhrmdPSPAVGTTMGNP---EFLQGPSVRPNY---GA 3094
Cdd:pfam09606   62 QPQGGQGNGGMGGGQQGMPDPiNALQNLAGQGTRPQMMGPMGPG----PGGPMGQQMGGPgtaSNLLASLGRPQMpmgGA 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3095 AGPQGEQIIPTGGQPMTHN---QQLMFSQGLNQQNRPLLLEEQPLLLQDLLDQERQEQQQQRQMQAMIRQRSNDSFFPni 3171
Cdd:pfam09606  138 GFPSQMSRVGRMQPGGQAGgmmQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADA-- 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3172 dfdaitdpimKAKMVALKGINKMMVQSSMGMPPMvmNRIQMGGQQGPEGVSAVPQQVIGQDGKLASQLPRRNPPNF--GP 3249
Cdd:pfam09606  216 ----------GAQMGQQAQANGGMNPQQMGGAPN--QVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGpgQP 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3250 GFVNDSQKKQYEEWLQHTQQLLKMQQKFLEEQIGAHRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSVVQKQLE 3329
Cdd:pfam09606  284 MGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAN 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3330 QIRKQQKEHAELIEEYRVKHLQcsMQQPPMVAGMQPQTVMLSGGPPINQPRMSPMMQM------QPYHN-----QPNAPR 3398
Cdd:pfam09606  364 PMQRGQPGMMSSPSPVPGQQVR--QVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMipspalIPSPSpqmsqQPAQQR 441
                          410       420
                   ....*....|....*....|....*...
gi 1658251387 3399 MsgIPGWHPGAP--RPIGPGVPAPMASQ 3424
Cdd:pfam09606  442 T--IGQDSPGGSlnTPGQSAVNSPLNPQ 467
PHA03089 super family cl28054
late transcription factor VLTF-4; Provisional
26-107 2.93e-03

late transcription factor VLTF-4; Provisional


The actual alignment was detected with superfamily member PHA02687:

Pssm-ID: 474989  Cd Length: 231  Bit Score: 42.69  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387   26 PVGSPTATDKRPRGRPRKDAAAATPKSRRKSRSRGKATADDEDsldgmETGETEITQEAGTKEAQGDGEGGEDSQSAEGP 105
Cdd:PHA02687    75 PESVPPAPVKTPKRRTKKKAKADKPEKSPKAVEKLCPPDDRDD-----KNEEKEPTEEAQRNEESGDAEGGASGRSPSDD 149

                   ..
gi 1658251387  106 DE 107
Cdd:PHA02687   150 DN 151
PRK05901 super family cl35405
RNA polymerase sigma factor; Provisional
2778-2900 8.06e-03

RNA polymerase sigma factor; Provisional


The actual alignment was detected with superfamily member PRK05901:

Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 42.29  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2778 TPADQPEDIAVNTEgIEEKLDTDDSAVKDLEDVEVKDLDDEDLENLNLDPDSTKELDLETSDLHLDDFLKSGKFDIIAYT 2857
Cdd:PRK05901    86 AAAKAPAKKKLKDE-LDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDDDD 164
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387 2858 DPDLDLGDK--KDMFNEELDLSDPIDDQSEASDLQKALSEKRNAS 2900
Cdd:PRK05901   165 VDDEDEEKKeaKELEKLSDDDDFVWDEDDSEALRQARKDAKLTAT 209
 
Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
4846-4998 9.79e-115

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


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 360.98  E-value: 9.79e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4846 KSSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVIDA 4925
Cdd:cd19171      1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4926 TITGGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWM 4998
Cdd:cd19171     81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
4488-4592 2.21e-72

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: 237.64  E-value: 2.21e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15697      1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80
                           90       100
                   ....*....|....*....|....*
gi 1658251387 4568 VYHFTCALKAQCTFFKDKTMLCHAH 4592
Cdd:cd15697     81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
HMG-box_KMT2C cd22026
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...
1663-1743 2.48e-55

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: 188.07  E-value: 2.48e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1663 QRSTLKWEKEETLGEMATVAPVLYTNMNFPNLKEEFPDWSTRVKQIAKLWRKASSQERSPYVQKARDNRAALRINKVQMS 1742
Cdd:cd22026      1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80

                   .
gi 1658251387 1743 N 1743
Cdd:cd22026     81 N 81
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
247-330 1.62e-44

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: 157.41  E-value: 1.62e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  247 GQCCAHQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFRKLTLL 326
Cdd:cd15696      7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86

                   ....
gi 1658251387  327 CPKH 330
Cdd:cd15696     87 CPTH 90
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
4860-4997 6.40e-37

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 137.40  E-value: 6.40e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4860 NVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRkekMYESQNRG-VYMFRIDSEHVIDATITGGPARYINHS 4938
Cdd:COG2940      7 RIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAER---REPHKEPLhTYLFELDDDGVIDGALGGNPARFINHS 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4939 CAPNCVAEvvtfEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHkiPCHCGavNCRKW 4997
Cdd:COG2940     84 CDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
4860-4981 3.53e-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: 132.07  E-value: 3.53e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  4860 NVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNR-GVYMFRIDSEHVIDATITGGPARYINHS 4938
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1658251387  4939 CAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDD 4981
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
PHD4_KMT2C cd15596
PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
937-992 6.16e-35

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: 128.98  E-value: 6.16e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387  937 FTMRQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLECT 992
Cdd:cd15596      2 FTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 57
PHD5_KMT2C_like cd15513
PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...
993-1039 9.89e-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: 113.73  E-value: 9.89e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCV 1039
Cdd:cd15513      1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47
PHD2_KMT2C cd15594
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
390-435 1.08e-28

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: 110.80  E-value: 1.08e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15594      1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
4870-4975 2.73e-28

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: 112.23  E-value: 2.73e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGT-IIRNEVANRKEKMYESQNR----GVYMFRID--SEHVIDATIT--GGPARYINHSCA 4940
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDedSEYCIDARALyyGNWARFINHSCD 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1658251387 4941 PNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYK 4975
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
PHD6_KMT2C cd15600
PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
1071-1120 1.86e-27

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: 107.32  E-value: 1.86e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1071 CPICCHDYRQDELIVQCRQCDRWMHACCQNLNSDEEVENVADDGFECAMC 1120
Cdd:cd15600      2 CPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC 51
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
4697-4780 2.24e-25

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: 102.69  E-value: 2.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4697 PEFIIRVVEQgyEDLVLKGTTPKGVWDQVLEQVAQHRTETGTLKLFPVYLKGEDLFGLTVSAVTRIIESLPGVEACENYA 4776
Cdd:pfam05965    2 PLFRVTVEED--PDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYK 79

                   ....
gi 1658251387 4777 FRYG 4780
Cdd:pfam05965   80 FRYG 83
PHD1_KMT2C_like cd15509
PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
343-388 6.26e-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: 97.38  E-value: 6.26e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  343 NCAVCDSPGDLLDQLFCTTCGQHYHGTCLDIGV--TPLKRAGWQCPEC 388
Cdd:cd15509      1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
4698-4785 7.10e-23

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: 95.44  E-value: 7.10e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  4698 EFIIRVVEQGyeDLVLKGTTPKGVWDQVLEQVAQHRTETGTLKLFPVYLKGEDLFGLTVSAVTRIIESLPGVEACENYAF 4777
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78

                    ....*...
gi 1658251387  4778 RYGRNPLM 4785
Cdd:smart00542   79 RYHRSPLL 86
PHA03247 PHA03247
large tegument protein UL36; Provisional
1893-2423 3.22e-20

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 100.40  E-value: 3.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1893 PTSGSLDDVFLRPQPPPPTGTRLTEAcsqgQASQPQSPQMFSTGTASSSSRPSSPWDPYAKMVGTPRPP------PIGSS 1966
Cdd:PHA03247  2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAapdrsvPPPRP 2573
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1967 TPRRNSTESCSAPRLPSEQQERGRPSSGHESFGSP----TSASVDPYAKPPDTPRPAVTADPFVKPMGPPKAGIVLEsQG 2042
Cdd:PHA03247  2574 APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPrgpaPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-RP 2652
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2043 RHMPASvigdAFARPSHRAEAYQRMSHNKMVLSDPySKPLLTPIPGSNESGSVPLFKAPMPPPHPQDLYNSTPSIGRRNS 2122
Cdd:PHA03247  2653 RDDPAP----GRVSRPRRARRLGRAAQASSPPQRP-RRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA 2727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2123 VDSFERPTRLsdtfsqnsqnDPYAHP-PLTPCTSMNDNFSNSPKMMHHPQSNA--FCQPMPMVRHPSRDAFAQASSTSRS 2199
Cdd:PHA03247  2728 ARQASPALPA----------APAPPAvPAGPATPGGPARPARPPTTAGPPAPAppAAPAAGPPRRLTRPAVASLSESRES 2797
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2200 DFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQ--PPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYS 2277
Cdd:PHA03247  2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPtaPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2278 PQQPSNRRSS---PSHAMEPYPQPPGTPCPgtgerfskspvsQRNADSyfqqPETPRlvkndtyaQQPNIPKPVLSDPYS 2354
Cdd:PHA03247  2878 PARPPVRRLArpaVSRSTESFALPPDQPER------------PPQPQA----PPPPQ--------PQPQPPPPPQPQPPP 2933
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 2355 QPPGTPRPGVGPEVFNRPVARTGPVSQDPFSSPQVTMQENFVRPQTPKHsglsddgfAQPQSNPASQTP 2423
Cdd:PHA03247  2934 PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQP--------APSREAPASSTP 2994
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
4639-4690 1.44e-17

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: 79.09  E-value: 1.44e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387 4639 GSLVLHTVGQLLPQQMAaFHGSSAIFPVGYESSRIYWSMRHGNRRCRYLCSI 4690
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPA-FHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
252-330 3.44e-16

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


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 76.60  E-value: 3.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  252 HQRCAVWSRGVCRGEGTSLL----NVDKAIDSGSTESCAYCK-RLGASIKCCQEECSRSYHYPCAAAAGTFQDF----RK 322
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSMGfpieDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFdednGT 80

                   ....*...
gi 1658251387  323 LTLLCPKH 330
Cdd:pfam13771   81 FKSYCKKH 88
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
4515-4592 2.19e-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: 74.29  E-value: 2.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4515 HLNCALWSTEVYetQAGA------LINVELALRRGLSIRCVYC-QRTGATSGCHRLRCTNVYHFTCALKAQCTF-FKDKT 4586
Cdd:pfam13771    1 HVVCALWSPELV--QRGNdsmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDN 78
                           90
                   ....*....|
gi 1658251387 4587 ----MLCHAH 4592
Cdd:pfam13771   79 gtfkSYCKKH 88
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
4649-4692 6.07e-15

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: 71.55  E-value: 6.07e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1658251387  4649 LLPQQMAAFHGSSAIFPVGYESSRIYWSMRHGNRRCRYLCSIDE 4692
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
993-1041 7.45e-13

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: 65.98  E-value: 7.45e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQT--VPKGSWKCKWCVSC 1041
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPaeIPSGEWLCPECKPK 51
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
390-438 1.63e-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: 64.82  E-value: 1.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDS--IPTNGWRCKNCRVC 438
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPaeIPSGEWLCPECKPK 51
PHD3_KMT2C cd15511
PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
469-519 8.48e-12

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: 62.89  E-value: 8.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  469 CPLCGKPLGAEFLSDHLTCQSCKRYLHLECERQAGGRTDPLDREGYICTLC 519
Cdd:cd15511      2 CPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
993-1038 4.48e-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: 60.69  E-value: 4.48e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1658251387   993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQT-VPKGSWKCKWC 1038
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
390-435 7.45e-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: 59.92  E-value: 7.45e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1658251387   390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDS-IPTNGWRCKNC 435
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
944-994 1.62e-10

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 59.04  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  944 CVVCGsfGQGAEGRLLACSQCGQCYHPYCVNIKITRVVLSKG-WRCLECTVC 994
Cdd:pfam00628    2 CAVCG--KSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
943-991 4.12e-10

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 57.99  E-value: 4.12e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1658251387   943 MCVVCGSFGqgAEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLEC 991
Cdd:smart00249    1 YCSVCGKPD--DGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
344-391 5.15e-10

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 57.89  E-value: 5.15e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  344 CAVCDSPGDLLDQLFCTTCGQHYHGTCLDIGVT--PLKRAGWQCPECKVC 391
Cdd:pfam00628    2 CAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDpaEIPSGEWLCPECKPK 51
PRK10263 PRK10263
DNA translocase FtsK; Provisional
2205-2754 6.29e-10

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 66.26  E-value: 6.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2205 SPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQ--------- 2275
Cdd:PRK10263   376 APEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAwqaeeqqst 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2276 YSPQ---QPSNRRSSPSHAMEPYPQPPGTPCPGTGErfsKSPVSQRNADS-----YFQQPETPRLVKNDTYAQ--QPnIP 2345
Cdd:PRK10263   456 FAPQstyQTEQTYQQPAAQEPLYQQPQPVEQQPVVE---PEPVVEETKPArpplyYFEEVEEKRAREREQLAAwyQP-IP 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2346 KPVlSDPYSQPPGTPRPGVGPEVFNRPVARTGPVSQdpfSSPQVTMqenfvrpqtpkHSGlSDDGFAQPQSNPASQTpvh 2425
Cdd:PRK10263   532 EPV-KEPEPIKSSLKAPSVAAVPPVEAAAAVSPLAS---GVKKATL-----------ATG-AAATVAAPVFSLANSG--- 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2426 dpyaqapmTPRPQ----LGDRLAREVKDQVEVGHEGSSHGVG----QFSNLQQSTSNSTESQSGAQLPLGDTEEkLRQRQ 2497
Cdd:PRK10263   593 --------GPRPQvkegIGPQLPRPKRIRVPTRRELASYGIKlpsqRAAEEKAREAQRNQYDSGDQYNDDEIDA-MQQDE 663
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2498 RLRELILRQQQQKSAIRQEKglqepsssipgTPRQWSQEETGQQNELfnrppppypgtARGSVISTGQRFPGLFPGeqrG 2577
Cdd:PRK10263   664 LARQFAQTQQQRYGEQYQHD-----------VPVNAEDADAAAEAEL-----------ARQFAQTQQQRYSGEQPA---G 718
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2578 AfqNEGQFPRAQFSADVANMGMRPPEPRFGfPSGGQVTLGGQGHFLRSPHHMQGPMIDVPQQMRRslsvdlsrtignnsl 2657
Cdd:PRK10263   719 A--NPFSLDDFEFSPMKALLDDGPHEPLFT-PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQ--------------- 780
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2658 llpqhfPPRSIPLQQHniMGQPFIELRHRAPENRVRLPFAPPAiagnvvdqsvQSQRPADPMLSQPsgitSHMQISSSME 2737
Cdd:PRK10263   781 ------PQQPVAPQPQ--YQQPQQPVAPQPQYQQPQQPVAPQP----------QYQQPQQPVAPQP----QYQQPQQPVA 838
                          570       580
                   ....*....|....*....|....
gi 1658251387 2738 NPHQQSL--PL-----NTEPQQAP 2754
Cdd:PRK10263   839 PQPQDTLlhPLlmrngDSRPLHKP 862
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
344-388 2.64e-08

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 52.98  E-value: 2.64e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1658251387   344 CAVCDSPGDLLDQLFCTTCGQHYHGTCLDI-GVTPLKRAGWQCPEC 388
Cdd:smart00249    2 CSVCGKPDDGGELLQCDGCDRWYHQTCLGPpLLEEEPDGKWYCPKC 47
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1861-2304 1.14e-07

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 58.63  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1861 SPMTPQP----TNGSTSPVQHMVPKDSLACSQLPGTPtsgslddvflrPQPPPPTGTRLTEACSQGQASQPQSPQMFSTG 1936
Cdd:pfam03154  145 SPSIPSPqdneSDSDSSAQQQILQTQPPVLQAQSGAA-----------SPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1937 TASSSSRPSSPWDPYAKMVGTPRPPPigsstprrnstescsaPRLPSEQqergrpssghesfgSPTSASVDPyaKPPDTP 2016
Cdd:pfam03154  214 TSQPPNQTQSTAAPHTLIQQTPTLHP----------------QRLPSPH--------------PPLQPMTQP--PPPSQV 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2017 RPAVTADPFVKPMGPPkAGIVLESQGRHMPASVIGDAFARPSHRAEAYQRMSHNKMVLSDPYSKPLLTPIPGSNESGS-- 2094
Cdd:pfam03154  262 SPQPLPQPSLHGQMPP-MPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQpp 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2095 --VPLFKAPMPPPHPQDlyNSTPSIGRRNSVDSFERPTRLS--DTFSQNSQNDPyaHPPLTPCTSMNDnfsnspkmmHHP 2170
Cdd:pfam03154  341 reQPLPPAPLSMPHIKP--PPTTPIPQLPNPQSHKHPPHLSgpSPFQMNSNLPP--PPALKPLSSLST---------HHP 407
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2171 QSnafCQPMPMVRHPSrdafaqasstsrsdfTQKSPDPYTQPPG---TPRPSDPYAQPPgTPRPAYDPYAQPPGTPRPFD 2247
Cdd:pfam03154  408 PS---AHPPPLQLMPQ---------------SQQLPPPPAQPPVltqSQSLPPPAASHP-PTSGLHQVPSQSPFPQHPFV 468
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387 2248 PYSKPPGTPrPASDSFSNSASRPGgvdqysPQQPSnrrSSPSHAMEPYPQPPGTPCP 2304
Cdd:pfam03154  469 PGGPPPITP-PSGPPTSTSSAMPG------IQPPS---SASVSSSGPVPAAVSCPLP 515
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
3355-3633 2.26e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 57.33  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3355 QQPPMVAGMQPQTVMLSGG---PPINQPRMSPMMQMQPYHNQPNAPRMSGIPGWHPGAPRPIGPGVPAPMASQAPSANTV 3431
Cdd:pfam09606  173 QMGPNGGPGQGQAGGMNGGqqgPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQG 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3432 QPVQTANGGGAPHvKFDDNNPFSEGFQERERKERLREQQERQRVQLMQEVERQRALQQRMEMEQQGLLGPDGNQDTLSQM 3511
Cdd:pfam09606  253 QQSQLGMGINQMQ-QMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMN 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3512 AFYG-----TDLPRDFM---QPQRPSAPQQMFPQQGVQPSFMSSSPGTFFMQTGERRPLIGngsfsseMGPSFRPKHLML 3583
Cdd:pfam09606  332 QSVGqggqvVALGGLNHletWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF-------MRQSPQPSVPSP 404
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 3584 QGPSFGPGQPRPPGFT-GPGMMPQGSadgPPFGVESATPLPPNYPGSGQSL 3633
Cdd:pfam09606  405 QGPGSQPPQSHPGGMIpSPALIPSPS---PQMSQQPAQQRTIGQDSPGGSL 452
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
2213-2446 2.96e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 53.62  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2213 PGTPRPsdPYAQPPGTPRPAYDPYAQPPGTPRPfdpysKPPGTPRPasdSFSNSASRPGgvDQYSPQQPSNRRSSPSHAM 2292
Cdd:NF033839   281 QDTPKE--PGNKKPSAPKPGMQPSPQPEKKEVK-----PEPETPKP---EVKPQLEKPK--PEVKPQPEKPKPEVKPQLE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2293 EPYPQ---PPGTPCPGTgerfskSPVSQRNADSYFQQPETPR-LVKNDTYAQQPNI-PKPVLSDPYSQP-PGTPRPGVGP 2366
Cdd:NF033839   349 TPKPEvkpQPEKPKPEV------KPQPEKPKPEVKPQPETPKpEVKPQPEKPKPEVkPQPEKPKPEVKPqPEKPKPEVKP 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2367 EVFN-RPVARTGPVSQDPFSSPQVTMQENFVRPQ--TPKHSGLSDDGFAQPQSNPASQTPVHDPYAQAPMTPRPQLGDRL 2443
Cdd:NF033839   423 QPEKpKPEVKPQPEKPKPEVKPQPEKPKPEVKPQpeTPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNL 502

                   ...
gi 1658251387 2444 ARE 2446
Cdd:NF033839   503 SKD 505
HMG smart00398
high mobility group;
1682-1735 3.67e-06

high mobility group;


Pssm-ID: 197700 [Multi-domain]  Cd Length: 70  Bit Score: 47.31  E-value: 3.67e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387  1682 APVLYTNMNFPNLKEEFPDWST--RVKQIAKLWRKASSQERSPYVQKARDNRAALR 1735
Cdd:smart00398    8 AFMLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
2001-2316 1.29e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 51.60  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2001 PTSASVDPYAKPP--DTPRPAVTADPFVKPMGPPKAGIVLESQGRHMPASVIGDAFARPSHRAEAYQRMSHNKMVLSDPY 2078
Cdd:COG5180    116 PELAAGALPAPAAaaALPKAKVTREATSASAGVALAAALLQRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRDALKDS 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2079 SKPLLTPIPGSNESGSVPLFKAPMPPPHPQDLYNSTP---------SIGRRNSVDSFERPTRLSDTFSQNSQ---NDPYA 2146
Cdd:COG5180    196 PEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAASSPkvdppstseARSRPATVDAQPEMRPPADAKERRRAaigDTPAA 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2147 HPPLTPCTSmndnfsNSPKmmhhPQSNAFCQPMPMVRHPSRDAFAQASSTSrsdftqKSPDPYTQPPGTPRPSDPYAQPP 2226
Cdd:COG5180    276 EPPGLPVLE------AGSE----PQSDAPEAETARPIDVKGVASAPPATRP------VRPPGGARDPGTPRPGQPTERPA 339
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2227 GTPRPAyDPYAQPPGTPRPFDP----YSKPPGTPRPASDSFSNSASRPGGVdqySPQQPSNRRSSPSHAMEPYPQPPGTP 2302
Cdd:COG5180    340 GVPEAA-SDAGQPPSAYPPAEEavpgKPLEQGAPRPGSSGGDGAPFQPPNG---APQPGLGRRGAPGPPMGAGDLVQAAL 415
                          330
                   ....*....|....
gi 1658251387 2303 CPGTGERFSKSPVS 2316
Cdd:COG5180    416 DGGGRETASLGGAA 429
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
4513-4622 4.10e-05

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 49.98  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4513 WVHLNCALWSTEVYETQAGALINVELALRRGLS---IRCVYCQ-RTGATSGCHRLRCTNVYHFTCALKAqCTFFK----- 4583
Cdd:COG5141    268 WGHVICAMFNPELSFGHLLSKDPIDNIASVSSSrwkLGCLICKeFGGTCIQCSYFNCTRAYHVTCARRA-GYFDLniysh 346
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387 4584 -------DKTMLCHAHKPRgGGGQEHELRYFAvFRRVYVQR--DEVRQ 4622
Cdd:COG5141    347 ngisyciDHEPLCRKHYPL-GYGRMNGLRYFG-YEKLRYKNppTAIPR 392
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
1070-1123 8.03e-05

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: 43.25  E-value: 8.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 1070 VCPICcHDYRQDELIVQCRQCDRWMHACCqnLNSDEEVENVADDGFECAMCHVR 1123
Cdd:pfam00628    1 YCAVC-GKSDDGGELVQCDGCDDWFHLAC--LGPPLDPAEIPSGEWLCPECKPK 51
HMG_box pfam00505
HMG (high mobility group) box;
1684-1735 9.06e-05

HMG (high mobility group) box;


Pssm-ID: 459837 [Multi-domain]  Cd Length: 68  Bit Score: 43.37  E-value: 9.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 1684 VLYTNMNFPNLKEEFPDWSTR--VKQIAKLWRKASSQERSPYVQKARDNRAALR 1735
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
3256-3348 5.89e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.60  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3256 QKKQYEEWLQHTQ-QLLKMQQKFLEEQIGAHR---KSKKALSAKQRTAKKAgREFpEEDAEQLKHVTEQQSVVQKQLE-Q 3330
Cdd:pfam20492    7 EKQELEERLKQYEeETKKAQEELEESEETAEEleeERRQAEEEAERLEQKR-QEA-EEEKERLEESAEMEAEEKEQLEaE 84
                           90
                   ....*....|....*...
gi 1658251387 3331 IRKQQKEHAELIEEYRVK 3348
Cdd:pfam20492   85 LAEAQEEIARLEEEVERK 102
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1070-1120 9.22e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 39.89  E-value: 9.22e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  1070 VCPICcHDYRQDELIVQCRQCDRWMHA-CCQnlnsDEEVENVADDGFECAMC 1120
Cdd:smart00249    1 YCSVC-GKPDDGGELLQCDGCDRWYHQtCLG----PPLLEEEPDGKWYCPKC 47
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
3022-3424 1.14e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.38  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3022 VPTDHSGPGAQGSQLAGMPQN-SSLLMAPGHIQEVEMNPSVTIGhrmdPSPAVGTTMGNP---EFLQGPSVRPNY---GA 3094
Cdd:pfam09606   62 QPQGGQGNGGMGGGQQGMPDPiNALQNLAGQGTRPQMMGPMGPG----PGGPMGQQMGGPgtaSNLLASLGRPQMpmgGA 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3095 AGPQGEQIIPTGGQPMTHN---QQLMFSQGLNQQNRPLLLEEQPLLLQDLLDQERQEQQQQRQMQAMIRQRSNDSFFPni 3171
Cdd:pfam09606  138 GFPSQMSRVGRMQPGGQAGgmmQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADA-- 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3172 dfdaitdpimKAKMVALKGINKMMVQSSMGMPPMvmNRIQMGGQQGPEGVSAVPQQVIGQDGKLASQLPRRNPPNF--GP 3249
Cdd:pfam09606  216 ----------GAQMGQQAQANGGMNPQQMGGAPN--QVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGpgQP 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3250 GFVNDSQKKQYEEWLQHTQQLLKMQQKFLEEQIGAHRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSVVQKQLE 3329
Cdd:pfam09606  284 MGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAN 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3330 QIRKQQKEHAELIEEYRVKHLQcsMQQPPMVAGMQPQTVMLSGGPPINQPRMSPMMQM------QPYHN-----QPNAPR 3398
Cdd:pfam09606  364 PMQRGQPGMMSSPSPVPGQQVR--QVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMipspalIPSPSpqmsqQPAQQR 441
                          410       420
                   ....*....|....*....|....*...
gi 1658251387 3399 MsgIPGWHPGAP--RPIGPGVPAPMASQ 3424
Cdd:pfam09606  442 T--IGQDSPGGSlnTPGQSAVNSPLNPQ 467
PHA02687 PHA02687
ORF061 late transcription factor VLTF-4; Provisional
26-107 2.93e-03

ORF061 late transcription factor VLTF-4; Provisional


Pssm-ID: 222918  Cd Length: 231  Bit Score: 42.69  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387   26 PVGSPTATDKRPRGRPRKDAAAATPKSRRKSRSRGKATADDEDsldgmETGETEITQEAGTKEAQGDGEGGEDSQSAEGP 105
Cdd:PHA02687    75 PESVPPAPVKTPKRRTKKKAKADKPEKSPKAVEKLCPPDDRDD-----KNEEKEPTEEAQRNEESGDAEGGASGRSPSDD 149

                   ..
gi 1658251387  106 DE 107
Cdd:PHA02687   150 DN 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3257-3344 4.56e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3257 KKQYEEwLQHTQQLLKMQQKFLEEQIGAHRKSKKALSAKQRTAKKAGREFP---EEDAEQLKHVTEQQSVVQKQLEQIRK 3333
Cdd:TIGR02168  280 EEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEA 358
                           90
                   ....*....|.
gi 1658251387 3334 QQKEHAELIEE 3344
Cdd:TIGR02168  359 ELEELEAELEE 369
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
246-317 7.60e-03

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 42.66  E-value: 7.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387  246 TGQCCaHQRCAVWSRGVCRGEGTSLLNVD--KAIDSGSTES-CAYCK-RLGASIKCCQEECSRSYHYPCAAAAGTF 317
Cdd:COG5141    265 DGRWG-HVICAMFNPELSFGHLLSKDPIDniASVSSSRWKLgCLICKeFGGTCIQCSYFNCTRAYHVTCARRAGYF 339
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
2778-2900 8.06e-03

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 42.29  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2778 TPADQPEDIAVNTEgIEEKLDTDDSAVKDLEDVEVKDLDDEDLENLNLDPDSTKELDLETSDLHLDDFLKSGKFDIIAYT 2857
Cdd:PRK05901    86 AAAKAPAKKKLKDE-LDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDDDD 164
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387 2858 DPDLDLGDK--KDMFNEELDLSDPIDDQSEASDLQKALSEKRNAS 2900
Cdd:PRK05901   165 VDDEDEEKKeaKELEKLSDDDDFVWDEDDSEALRQARKDAKLTAT 209
 
Name Accession Description Interval E-value
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
4846-4998 9.79e-115

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


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 360.98  E-value: 9.79e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4846 KSSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVIDA 4925
Cdd:cd19171      1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4926 TITGGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWM 4998
Cdd:cd19171     81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
4845-4998 9.29e-104

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: 329.67  E-value: 9.29e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4845 SKSSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVID 4924
Cdd:cd19208      1 SKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVID 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 4925 ATITGGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWM 4998
Cdd:cd19208     81 ATLTGGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 154
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
4844-4998 5.28e-92

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: 295.84  E-value: 5.28e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4844 HSKSSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVI 4923
Cdd:cd19209      1 HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658251387 4924 DATITGGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWM 4998
Cdd:cd19209     81 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
4488-4592 2.21e-72

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: 237.64  E-value: 2.21e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15697      1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80
                           90       100
                   ....*....|....*....|....*
gi 1658251387 4568 VYHFTCALKAQCTFFKDKTMLCHAH 4592
Cdd:cd15697     81 VYHFTCAIKAQCMFFKDKTMLCPMH 105
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
4847-4995 1.61e-70

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: 234.03  E-value: 1.61e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4847 SSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQN-RGVYMFRIDSEHVIDA 4925
Cdd:cd10518      2 SKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVIDA 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4926 TITGGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQhKIPCHCGAVNCR 4995
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); ...
4488-4592 1.76e-66

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: 220.64  E-value: 1.76e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15666      1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80
                           90       100
                   ....*....|....*....|....*
gi 1658251387 4568 VYHFTCALKAQCTFFKDKTMLCHAH 4592
Cdd:cd15666     81 VYHLPCAIKDGCMFFKDKTMLCPSH 105
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
4488-4593 1.14e-62

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: 209.91  E-value: 1.14e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15698      1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80
                           90       100
                   ....*....|....*....|....*.
gi 1658251387 4568 VYHFTCALKAQCTFFKDKTMLCHAHK 4593
Cdd:cd15698     81 VYHFACAIRAKCMFFKDKTMLCPMHK 106
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
4847-4999 5.64e-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: 204.16  E-value: 5.64e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4847 SSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVIDAT 4926
Cdd:cd19170      2 AMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDAT 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4927 ITGGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDqhKIPCHCGAVNCRKWMN 4999
Cdd:cd19170     82 MHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDV--KIPCTCGSKKCRKYLN 152
HMG-box_KMT2C cd22026
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...
1663-1743 2.48e-55

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: 188.07  E-value: 2.48e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1663 QRSTLKWEKEETLGEMATVAPVLYTNMNFPNLKEEFPDWSTRVKQIAKLWRKASSQERSPYVQKARDNRAALRINKVQMS 1742
Cdd:cd22026      1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQMS 80

                   .
gi 1658251387 1743 N 1743
Cdd:cd22026     81 N 81
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
4858-4995 2.14e-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: 187.93  E-value: 2.14e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRG-VYMFRIDSEHVIDATITGGPARYIN 4936
Cdd:cd19169     12 KKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGsSYLFRVDDDTIIDATKCGNLARFIN 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4937 HSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDqhKIPCHCGAVNCR 4995
Cdd:cd19169     92 HSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDE--KIPCLCGAPQCR 148
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
4849-4999 3.68e-48

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: 170.59  E-value: 3.68e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4849 QYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVIDATIT 4928
Cdd:cd19206      4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDATMH 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 4929 GGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWMN 4999
Cdd:cd19206     84 GNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
4858-4995 3.96e-48

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: 169.91  E-value: 3.96e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRG-VYMFRIDSEHVIDATITGGPARYIN 4936
Cdd:cd20072     12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDATKKGNIARFIN 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4937 HSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDqhKIPCHCGAVNCR 4995
Cdd:cd20072     92 HCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREED--KIPCLCGAPNCR 148
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
247-330 1.62e-44

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: 157.41  E-value: 1.62e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  247 GQCCAHQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFRKLTLL 326
Cdd:cd15696      7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86

                   ....
gi 1658251387  327 CPKH 330
Cdd:cd15696     87 CPTH 90
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
4849-4999 4.10e-43

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: 155.95  E-value: 4.10e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4849 QYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVIDATIT 4928
Cdd:cd19207      4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 4929 GGPARYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWMN 4999
Cdd:cd19207     84 GNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 154
HMG_KMT2C-like cd21997
high mobility group (HMG)-box found in histone-lysine N-methyltransferases KMT2C, KMT2D and ...
1668-1734 2.45e-40

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: 144.81  E-value: 2.45e-40
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387 1668 KWEKEETLGEMATVAPVLYTNMNFPNLKEEFPDWSTRVKQIAKLWRKASSQERSPYVQKARDNRAAL 1734
Cdd:cd21997      1 KWEKDEPLGDMATISPVLYANINHPNLKQEYPDWTDRAKQIAKLWRKLSAEERAPYLQKARENRAAL 67
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
4858-4999 4.86e-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: 144.40  E-value: 4.86e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGV-YMFRIDSEHVIDATITGGPARYIN 4936
Cdd:cd19204     13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLARFIN 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4937 HSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDqhKIPCHCGAVNCRKWMN 4999
Cdd:cd19204     93 HCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIEDN--KIPCLCGTENCRGTLN 153
HMG-box_KMT2D cd22027
high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and ...
1659-1740 5.66e-39

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: 141.38  E-value: 5.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1659 MSNAQRSTLKWEKEETLGEMATVAPVLYTNMNFPNLKEEFPDWSTRVKQIAKLWRKASSQERSPYVQKARDNRAALRINK 1738
Cdd:cd22027      2 LSYNQRSLQRWEKDEELGELSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINK 81

                   ..
gi 1658251387 1739 VQ 1740
Cdd:cd22027     82 VQ 83
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
4858-4999 5.62e-38

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: 141.35  E-value: 5.62e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGV-YMFRIDSEHVIDATITGGPARYIN 4936
Cdd:cd19205     13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDATKCGNFARFIN 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4937 HSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDqhKIPCHCGAVNCRKWMN 4999
Cdd:cd19205     93 HSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDV--KIPCLCGSENCRGTLN 153
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
4860-4997 6.40e-37

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 137.40  E-value: 6.40e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4860 NVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRkekMYESQNRG-VYMFRIDSEHVIDATITGGPARYINHS 4938
Cdd:COG2940      7 RIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAER---REPHKEPLhTYLFELDDDGVIDGALGGNPARFINHS 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4939 CAPNCVAEvvtfEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHkiPCHCGavNCRKW 4997
Cdd:COG2940     84 CDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
247-330 8.98e-37

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: 135.14  E-value: 8.98e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  247 GQCCAHQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFRKLTLL 326
Cdd:cd15665      7 GEVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGCFQDIKTLTLF 86

                   ....
gi 1658251387  327 CPKH 330
Cdd:cd15665     87 CPEH 90
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
4488-4592 2.42e-35

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: 131.76  E-value: 2.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15664      1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80
                           90       100
                   ....*....|....*....|....*
gi 1658251387 4568 VYHFTCALKAQCTFFKDKTMLCHAH 4592
Cdd:cd15664     81 NYHFMCARKAECVFQDDKKVFCPAH 105
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
4860-4981 3.53e-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: 132.07  E-value: 3.53e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  4860 NVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNR-GVYMFRIDSEHVIDATITGGPARYINHS 4938
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1658251387  4939 CAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDD 4981
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
PHD4_KMT2C cd15596
PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
937-992 6.16e-35

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: 128.98  E-value: 6.16e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387  937 FTMRQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLECT 992
Cdd:cd15596      2 FTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECT 57
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
4486-4593 1.12e-32

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: 124.73  E-value: 1.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4486 RKCCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRC 4565
Cdd:cd15693      1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80
                           90       100
                   ....*....|....*....|....*...
gi 1658251387 4566 TNVYHFTCALKAQCTFFKDKTMLCHAHK 4593
Cdd:cd15693     81 TSNYHFMCSRAKNCVFLEDKKVYCQRHK 108
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
4854-4998 2.58e-30

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: 118.84  E-value: 2.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4854 KTEWKtnvylarsriqGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMF-RIDSEHVIDATITGGPA 4932
Cdd:cd19172      8 RTEKK-----------GWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFmALKSDEIIDATKKGNLS 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387 4933 RYINHSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKiPCHCGAVNCRKWM 4998
Cdd:cd19172     77 RFINHSCEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFERYGKEAQ-KCYCGSPNCRGYI 141
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
4870-4998 2.62e-30

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: 122.40  E-value: 2.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRgVYMFRID-----SEHVIDATITGGPARYINHSCAPN-- 4942
Cdd:cd10542     99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDyndddCEYTVDAAYYGNISHFINHSCDPNla 177
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4943 ---CVAEVVtFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQH----------KIPCHCGAVNCRKWM 4998
Cdd:cd10542    178 vyaVWINHL-DPRLPRIAFFAKRDIKAGEELTFDYLMTGTGGSSestipkpkdvRVPCLCGSKNCRKYL 245
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
4870-4998 6.64e-30

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: 117.52  E-value: 6.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQ-NRGVYMFRIDSEHVIDATITGGPARYINHSCAPNCVAEVV 4948
Cdd:cd19175     11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKgEKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 4949 TFEKGHKIIISSNRKIQRGEELCYDYKF-DLEDDQHkipCHCGAVNCRKWM 4998
Cdd:cd19175     91 QVDGETRIGVFAIRDIKKGEELTYDYQFvQFGADQD---CHCGSKNCRGKL 138
PHD5_KMT2C_like cd15513
PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...
993-1039 9.89e-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: 113.73  E-value: 9.89e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCV 1039
Cdd:cd15513      1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
4860-4995 1.09e-29

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: 116.97  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4860 NVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRK-EKMYESQNRGVYMFRIDSEHVIDATITGGPARYINHS 4938
Cdd:cd10531      1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERlDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFINHS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 4939 CAPNCVAEvVTFEKGHKII-ISSNRKIQRGEELCYDYKFDLEDDQhKIPCHCGAVNCR 4995
Cdd:cd10531     81 CEPNCETQ-KWIVNGEYRIgIFALRDIPAGEELTFDYNFVNYNEA-KQVCLCGAQNCR 136
PHD4_KMT2C_like cd15512
PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD domain 3 found in ...
943-991 1.67e-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: 112.94  E-value: 1.67e-29
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1658251387  943 MCVVCGSFGQGAEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLEC 991
Cdd:cd15512      1 MCVSCGSFGRGAEGRLIACSQCGQCYHPYCVNVKVTKVILSKGWRCLDC 49
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
4861-4974 2.80e-29

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: 115.03  E-value: 2.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4861 VYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGvYMFRIDSEHVIDATITGGPARYINHSCA 4940
Cdd:cd10519      3 LLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSN 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1658251387 4941 PNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd10519     82 PNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDY 115
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
247-330 3.36e-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: 113.86  E-value: 3.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  247 GQCCAHQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFRKLTLL 326
Cdd:cd15695      7 GECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGSFQSMKTLLLL 86

                   ....
gi 1658251387  327 CPKH 330
Cdd:cd15695     87 CPEH 90
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
4858-4994 6.71e-29

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


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 114.72  E-value: 6.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRiqGLGLYAARDIEKYTMVIEYIGTII-RNEVANRKEKMYESQNRGVYMFRIDSEHVIDATITGGPARYIN 4936
Cdd:cd19173      3 PTEPFKTGDR--GWGLRTKRDIKKGDFVIEYVGELIdEEECRRRLKKAHENNITNFYMLTLDKDRIIDAGPKGNLSRFMN 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 4937 HSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQhKIPCHCGAVNC 4994
Cdd:cd19173     81 HSCQPNCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNE-KKVCRCGAPNC 137
PHD2_KMT2C cd15594
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
390-435 1.08e-28

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: 110.80  E-value: 1.08e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15594      1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
4870-4975 2.73e-28

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: 112.23  E-value: 2.73e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGT-IIRNEVANRKEKMYESQNR----GVYMFRID--SEHVIDATIT--GGPARYINHSCA 4940
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDedSEYCIDARALyyGNWARFINHSCD 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1658251387 4941 PNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYK 4975
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
4488-4592 1.02e-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: 110.13  E-value: 1.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15694      1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80
                           90       100
                   ....*....|....*....|....*
gi 1658251387 4568 VYHFTCALKAQCTFFKDKTMLCHAH 4592
Cdd:cd15694     81 NFHFMCARASRCCFQDDKKVFCQKH 105
PHD6_KMT2C cd15600
PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
1071-1120 1.86e-27

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: 107.32  E-value: 1.86e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1071 CPICCHDYRQDELIVQCRQCDRWMHACCQNLNSDEEVENVADDGFECAMC 1120
Cdd:cd15600      2 CPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC 51
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
4488-4592 2.18e-27

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors.


Pssm-ID: 277046 [Multi-domain]  Cd Length: 112  Bit Score: 109.21  E-value: 2.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPArLLNLDLDLWVHLNCALWSTEVYETQAGAL--INVELALRRGLSIRCVYCQRT-GATSGCHRLR 4564
Cdd:cd15571      1 CALCPRSGGALKGGGA-LKTTSDGLWVHVVCALWSPEVYFDDGTLLevEGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1658251387 4565 CTNVYHFTCALKAQCTF-----FKDKTMLCHAH 4592
Cdd:cd15571     80 CPRSFHVSCAIRAGCLFefedgPGNFVVYCPKH 112
PHD3_KMT2D cd15597
PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
942-991 3.02e-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: 106.66  E-value: 3.02e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  942 DMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLEC 991
Cdd:cd15597      1 DMCVVCGSFGRGSEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 50
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
4697-4780 2.24e-25

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: 102.69  E-value: 2.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4697 PEFIIRVVEQgyEDLVLKGTTPKGVWDQVLEQVAQHRTETGTLKLFPVYLKGEDLFGLTVSAVTRIIESLPGVEACENYA 4776
Cdd:pfam05965    2 PLFRVTVEED--PDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYK 79

                   ....
gi 1658251387 4777 FRYG 4780
Cdd:pfam05965   80 FRYG 83
PHD2_KMT2C_like cd15510
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
390-435 4.90e-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: 100.20  E-value: 4.90e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15510      1 VCQACRQPGDDTKMLVCETCDKGYHTSCLRPVMSSIPKYGWKCKNC 46
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
4870-4999 7.46e-25

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: 103.14  E-value: 7.46e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGTII-RNEVANRKEKMYeSQNRGVYMFRIDSEHVIDATITGGPARYINHSCAPNCVAEVV 4948
Cdd:cd19174     11 GWGVRTKEPIKAGQFIIEYVGEVVsEQEFRRRMIEQY-HNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSCDPNCEMQKW 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 4949 TFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHCGAVNCRKWMN 4999
Cdd:cd19174     90 SVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG 140
PHD2_KMT2D cd15595
PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
390-435 1.99e-24

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: 98.53  E-value: 1.99e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15595      1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46
PHD1_KMT2C_like cd15509
PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
343-388 6.26e-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: 97.38  E-value: 6.26e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  343 NCAVCDSPGDLLDQLFCTTCGQHYHGTCLDIGV--TPLKRAGWQCPEC 388
Cdd:cd15509      1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
4698-4785 7.10e-23

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: 95.44  E-value: 7.10e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  4698 EFIIRVVEQGyeDLVLKGTTPKGVWDQVLEQVAQHRTETGTLKLFPVYLKGEDLFGLTVSAVTRIIESLPGVEACENYAF 4777
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78

                    ....*...
gi 1658251387  4778 RYGRNPLM 4785
Cdd:smart00542   79 RYHRSPLL 86
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
4857-4976 1.39e-21

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: 93.05  E-value: 1.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4857 WKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYEsQNRGVYMFRIDSEHVIDATITGGPARYIN 4936
Cdd:cd19218      2 SKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFAN 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1658251387 4937 HSCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKF 4976
Cdd:cd19218     81 HSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120
PHD6_KMT2C_like cd15514
PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in ...
1070-1120 5.61e-21

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: 88.88  E-value: 5.61e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 1070 VCPICCHDYRQDELIVQCRQCDRWMHACCQNLNSDEEVENVADDGFECAMC 1120
Cdd:cd15514      1 KCPVCSRSYNEGELIIQCSQCERWLHGACDSLRTEEEAERAADNGYRCLLC 51
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
4858-4980 2.89e-20

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: 90.13  E-value: 2.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYEsQNRGVYMFRIDSEHVIDATITGGPARYINH 4937
Cdd:cd19217      5 KKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANH 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1658251387 4938 SCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLED 4980
Cdd:cd19217     84 SVNPNCYAKVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQAD 126
PHA03247 PHA03247
large tegument protein UL36; Provisional
1893-2423 3.22e-20

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 100.40  E-value: 3.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1893 PTSGSLDDVFLRPQPPPPTGTRLTEAcsqgQASQPQSPQMFSTGTASSSSRPSSPWDPYAKMVGTPRPP------PIGSS 1966
Cdd:PHA03247  2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAapdrsvPPPRP 2573
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1967 TPRRNSTESCSAPRLPSEQQERGRPSSGHESFGSP----TSASVDPYAKPPDTPRPAVTADPFVKPMGPPKAGIVLEsQG 2042
Cdd:PHA03247  2574 APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPrgpaPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-RP 2652
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2043 RHMPASvigdAFARPSHRAEAYQRMSHNKMVLSDPySKPLLTPIPGSNESGSVPLFKAPMPPPHPQDLYNSTPSIGRRNS 2122
Cdd:PHA03247  2653 RDDPAP----GRVSRPRRARRLGRAAQASSPPQRP-RRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA 2727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2123 VDSFERPTRLsdtfsqnsqnDPYAHP-PLTPCTSMNDNFSNSPKMMHHPQSNA--FCQPMPMVRHPSRDAFAQASSTSRS 2199
Cdd:PHA03247  2728 ARQASPALPA----------APAPPAvPAGPATPGGPARPARPPTTAGPPAPAppAAPAAGPPRRLTRPAVASLSESRES 2797
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2200 DFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQ--PPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYS 2277
Cdd:PHA03247  2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPtaPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2278 PQQPSNRRSS---PSHAMEPYPQPPGTPCPgtgerfskspvsQRNADSyfqqPETPRlvkndtyaQQPNIPKPVLSDPYS 2354
Cdd:PHA03247  2878 PARPPVRRLArpaVSRSTESFALPPDQPER------------PPQPQA----PPPPQ--------PQPQPPPPPQPQPPP 2933
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 2355 QPPGTPRPGVGPEVFNRPVARTGPVSQDPFSSPQVTMQENFVRPQTPKHsglsddgfAQPQSNPASQTP 2423
Cdd:PHA03247  2934 PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQP--------APSREAPASSTP 2994
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
4863-4994 6.80e-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: 89.28  E-value: 6.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4863 LARSRIQGLGLYAARDIEKYTMVIEYIGTII-RNEVANRKEKMYESQNRGVYMFRIDSEHVIDATITGGPARYINHSCAP 4941
Cdd:cd19211      6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIdEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQP 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4942 NCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIpCHCGAVNC 4994
Cdd:cd19211     86 NCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTV-CRCGAPNC 137
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
4870-4974 1.72e-19

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: 87.01  E-value: 1.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNrgvYMFRIDSEH-VIDATITGGPARYINHSCAPNCVAEVV 4948
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPL---YPFDLNGDIlVIDAGKKGNLTRFINHSDQPNLELIVR 90
                           90       100
                   ....*....|....*....|....*.
gi 1658251387 4949 TFEKGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd10522     91 TLKGEQHIGFVAIRDIKPGEELFISY 116
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
251-330 3.32e-19

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: 86.10  E-value: 3.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  251 AHQRCAVWSRGVCRGEGTSLL--NVDKAIDSGSTESCAYC-KRLGASIKCCQEECSRSYHYPCAAAAGTFQDFR----KL 323
Cdd:cd15571     26 VHVVCALWSPEVYFDDGTLLEveGVSKIPKRRKKLKCSICgKRGGACIQCSYPGCPRSFHVSCAIRAGCLFEFEdgpgNF 105

                   ....*..
gi 1658251387  324 TLLCPKH 330
Cdd:cd15571    106 VVYCPKH 112
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
4488-4592 4.96e-19

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


Pssm-ID: 277138  Cd Length: 103  Bit Score: 85.05  E-value: 4.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFC--HEEGDGLTD--GPArllnldLDLWVHLNCALWSTEVYETqAGALINVELALRRGLSIRCVYCQRTGATSGCHRL 4563
Cdd:cd15668      1 CVFCkrGPHYKGLGDlfGPY------YEVWVHEDCAVWAPGVYLV-GGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHK 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 1658251387 4564 RCTNVYHFTCALKAQCTFFKDK-TMLCHAH 4592
Cdd:cd15668     74 GCKAKYHYPCAVESGCQLDEENfSLLCPKH 103
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
252-330 6.61e-19

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: 85.05  E-value: 6.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  252 HQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGT--FQDfrKlTLLCPK 329
Cdd:cd15666     28 HLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGCmfFKD--K-TMLCPS 104

                   .
gi 1658251387  330 H 330
Cdd:cd15666    105 H 105
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
4870-4998 2.01e-18

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: 88.12  E-value: 2.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKmyeSQNRGV--YMFRIdSEHV---------IDATITGGPARYINHS 4938
Cdd:cd10544    101 GWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTK---SQTKGDmnYIIVL-REHLssgkvletfVDPTYIGNIGRFLNHS 176
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 4939 CAPNC------VAEVVTfekghKIIISSNRKIQRGEELCYDY------------KFDLEDDQHKIPCHCGAVNCRKWM 4998
Cdd:cd10544    177 CEPNLfmvpvrVDSMVP-----KLALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSRKPCLCGAENCRGFL 249
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
4858-4974 2.72e-18

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: 87.04  E-value: 2.72e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYeSQNRGVYMFRIDS---------EHVIDATIT 4928
Cdd:cd10538     88 QARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIY-DKSGGSYLFDLDEfsdsdgdgeELCVDATFC 166
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4929 GGPARYINHSCAPN----CVAEVVTFEKGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd10538    167 GNVSRFINHSCDPNlfpfNVVIDHDDLRYPRIALFATRDILPGEELTFDY 216
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
4867-4974 3.90e-18

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: 83.78  E-value: 3.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4867 RIQGLGLYAARDIEKYTMVIEYIGTII-RNEVANRKEKMYESQNRGVYM--FRIDSE-HVIDAT-ITGGPARYINHSC-A 4940
Cdd:cd10528     25 DGKGRGVIATRPFEKGDFVVEYHGDLItITEAKKREALYAKDPSTGCYMyyFQYKGKtYCVDATkESGRLGRLINHSKkK 104
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1658251387 4941 PNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd10528    105 PNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138
PHD5_KMT2D cd15601
PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
1071-1120 7.07e-18

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: 79.95  E-value: 7.07e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1071 CPICCHDYRQDELIVQCRQCDRWMHACCQNLNSDEEVENVADDGFECAMC 1120
Cdd:cd15601      2 CPVCRAKYVEEDLLIQCRHCDRWVHAVCESLFTEDEVEQAADEGFDCSSC 51
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
4869-4998 1.30e-17

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: 86.09  E-value: 1.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4869 QGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYEsqNRGV-YMFRID-------SEHVIDATITGGPARYINHSCA 4940
Cdd:cd20073    103 KGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYD--NVGVtYLFDLDlfedqvdEYYTVDAQYCGDVTRFINHSCD 180
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 4941 PNCVAEVVTFEKGHKIIIS----SNRKIQRGEELCYDYKFDLEDDQ----------------HKIPCHCGAVNCRKWM 4998
Cdd:cd20073    181 PNLAIYSVLRDKSDSKIYDlaffAIKDIPALEELTFDYSGRNNFDQlgfignrsnskyinlkNKRPCYCGSANCRGWL 258
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
4639-4690 1.44e-17

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: 79.09  E-value: 1.44e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387 4639 GSLVLHTVGQLLPQQMAaFHGSSAIFPVGYESSRIYWSMRHGNRRCRYLCSI 4690
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPA-FHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
4869-4994 6.36e-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: 80.74  E-value: 6.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4869 QGLGLYAARDIEKYTMVIEYIGTII-RNEVANRKEKMYESQNRGVYMFRIDSEHVIDATITGGPARYINHSCAPNCVAEV 4947
Cdd:cd19212     12 RGWGLRTKRSIKKGEFVNEYVGELIdEEECRLRIKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQK 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387 4948 VTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIpCHCGAVNC 4994
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); ...
4488-4592 6.36e-17

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


Pssm-ID: 277135  Cd Length: 90  Bit Score: 78.52  E-value: 6.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCheegdgltdgparllNLDlDLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTN 4567
Cdd:cd15665      1 CALC---------------NLG-EVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSK 64
                           90       100
                   ....*....|....*....|....*..
gi 1658251387 4568 VYHFTCALKAQCtF--FKDKTMLCHAH 4592
Cdd:cd15665     65 SFHFPCAAAAGC-FqdIKTLTLFCPEH 90
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
242-330 2.12e-16

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: 77.73  E-value: 2.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  242 LFDPTGQCCAHQRCAVWSRGVCRGeGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFR 321
Cdd:cd15668     16 LFGPYYEVWVHEDCAVWAPGVYLV-GGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEE 94

                   ....*....
gi 1658251387  322 KLTLLCPKH 330
Cdd:cd15668     95 NFSLLCPKH 103
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
252-330 3.44e-16

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


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 76.60  E-value: 3.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  252 HQRCAVWSRGVCRGEGTSLL----NVDKAIDSGSTESCAYCK-RLGASIKCCQEECSRSYHYPCAAAAGTFQDF----RK 322
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSMGfpieDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFdednGT 80

                   ....*...
gi 1658251387  323 LTLLCPKH 330
Cdd:pfam13771   81 FKSYCKKH 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
1862-2390 5.08e-16

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 86.53  E-value: 5.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1862 PMTPQPTNGSTSPVQHMVPKDSLACSQLPGTPTSGSLDDVFLRPQPPPPTGTRLTEACSQGQASQPQSPQMFSTGTASSS 1941
Cdd:PHA03247  2611 PAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARP 2690
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1942 S--RPSSPWDPYA-KMVGTPRPPPIGSSTPRRNSTESC--SAPRLPSEQQERGRPSsghesfGSPTSASVDPYAKPPDTP 2016
Cdd:PHA03247  2691 TvgSLTSLADPPPpPPTPEPAPHALVSATPLPPGPAAArqASPALPAAPAPPAVPA------GPATPGGPARPARPPTTA 2764
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2017 RPAVTADPFVKPMGPPKAGIvlesqgRHMPASVIGDAFARPSHRAEAYQRMSHNKMVLSDPYSKPLLTPIPGSNESGSVP 2096
Cdd:PHA03247  2765 GPPAPAPPAAPAAGPPRRLT------RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2097 LFKAPMPPPHPQDLYNSTPSIGrrnsvDSFERPtrlsdtfsqnsqndPYAHPPLTPCTSmndnfsnspkmmHHPQSNAFC 2176
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGG-----DVRRRP--------------PSRSPAAKPAAP------------ARPPVRRLA 2887
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2177 QPMPmvrHPSRDAFAQAsstsrsdftQKSPDPYTQPPGTPRPSD-PYAQPPGTPRPAYDPYAQPPGTPRPfDPYSKPPGT 2255
Cdd:PHA03247  2888 RPAV---SRSTESFALP---------PDQPERPPQPQAPPPPQPqPQPPPPPQPQPPPPPPPRPQPPLAP-TTDPAGAGE 2954
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2256 PRPASDSFSNSASRPGGVDQYSPQQPSNRRSSPSHAmEPYPQPPGTPCPGTG---------ERFSKSPVS---------- 2316
Cdd:PHA03247  2955 PSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPA-SSTPPLTGHSLSRVSswasslalhEETDPPPVSlkqtlwppdd 3033
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387 2317 --QRNADS-YFQQPEtprlvKNDTYAQQPNIPKPvlSDPYSQPPGTPRPGVGpevfnrpvARTGPVSQdpFSSPQVT 2390
Cdd:PHA03247  3034 teDSDADSlFDSDSE-----RSDLEALDPLPPEP--HDPFAHEPDPATPEAG--------ARESPSSQ--FGPPPLS 3093
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
4858-4995 1.19e-15

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: 79.69  E-value: 1.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4858 KTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKmyESqnrgvYMFRIDSE----HVIDATITGGPAR 4933
Cdd:cd10543     90 RYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRED--DS-----YLFDLDNKdgetYCIDARRYGNISR 162
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4934 YINHSCAPNCVAevVTFEKGH------KIIISSNRKIQRGEELCYDYKFDLEDDQHK-IPCHCGAVNCR 4995
Cdd:cd10543    163 FINHLCEPNLIP--VRVFVEHqdlrfpRIAFFASRDIKAGEELGFDYGEKFWRIKGKyFTCRCGSPKCK 229
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
4861-4974 1.41e-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: 1.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4861 VYLARSRIQ-GLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRgVYMFRIDSEHVIDATITGGPARYINH-- 4937
Cdd:cd19168      3 VVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVSY-LYLFEEQEGIWVDAAIYGNLSRYINHat 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1658251387 4938 --SCAPNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd19168     82 dkVKTGNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
4870-4998 1.70e-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: 80.05  E-value: 1.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGTIIRNEVAN-RKEKMYESQNRGVYMFRID--------------SEHVIDATITGGPARY 4934
Cdd:cd19473    117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQrRRDAATIAQRKDVYLFALDkfsdpdsldprlrgDPYEIDGEFMSGPTRF 196
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 4935 INHSCAPNC-VAEVVT--FEKG-HKIIISSNRKIQRGEELCYDY----------KFDLEDDQHKIPCHCGAVNCRKWM 4998
Cdd:cd19473    197 INHSCDPNLrIFARVGdhADKHiHDLAFFAIKDIPRGTELTFDYvdgvtgldddAGDEEKEKEMTKCLCGSPKCRGYL 274
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
4515-4592 2.19e-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: 74.29  E-value: 2.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4515 HLNCALWSTEVYetQAGA------LINVELALRRGLSIRCVYC-QRTGATSGCHRLRCTNVYHFTCALKAQCTF-FKDKT 4586
Cdd:pfam13771    1 HVVCALWSPELV--QRGNdsmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDN 78
                           90
                   ....*....|
gi 1658251387 4587 ----MLCHAH 4592
Cdd:pfam13771   79 gtfkSYCKKH 88
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
4860-4974 2.91e-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: 73.44  E-value: 2.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4860 NVYLARSRIQGLGLYAARDIEKytmvieyiGTIIrnevanrkekmyesqnrgvymfridsehvidatitgGPARYINHSC 4939
Cdd:cd08161      1 EIRPSTIPGAGFGLFATRDIPK--------GEVI------------------------------------GLARFINHSC 36
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1658251387 4940 APNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd08161     37 EPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71
PHD1_Lid2p_like cd15519
PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...
993-1038 3.22e-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: 72.50  E-value: 3.22e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15519      1 GCEVCGLDDNEGEVLLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC 46
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
4861-4994 3.59e-15

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: 75.73  E-value: 3.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4861 VYLARSRIQGLGLYAARDIEKYTMVIEYIGTII-RNEVANRKEKMYESQNRGVYMFRIDSEHVIDATITGGPARYINHSC 4939
Cdd:cd19210      4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIdEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCC 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658251387 4940 APNCVAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQhKIPCHCGAVNC 4994
Cdd:cd19210     84 QPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNG-KTVCKCGAPNC 137
PHD1_KDM5B cd15603
PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis ...
993-1038 4.86e-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: 4.86e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15603      1 VCLVCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC 46
PHD1_KDM5A_like cd15515
PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...
993-1038 5.79e-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: 71.65  E-value: 5.79e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15515      1 ICQVCGRGDDEDKLLLCDGCDDSYHTFCLIPPLPDIPPGDWRCPKC 46
FYRN smart00541
FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...
4649-4692 6.07e-15

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: 71.55  E-value: 6.07e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1658251387  4649 LLPQQMAAFHGSSAIFPVGYESSRIYWSMRHGNRRCRYLCSIDE 4692
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
4869-4998 8.38e-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: 77.24  E-value: 8.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4869 QGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRgVYMFRID---SEHVIDATITGGPARYINHSCAPNCVA 4945
Cdd:cd10532     95 RGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGI-TYLFDLDyesDEFTVDAARYGNVSHFVNHSCDPNLQV 173
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4946 EVVTFE----KGHKIIISSNRKIQRGEELCYDYKF----DLEDD---------QHKIPCHCGAVNCRKWM 4998
Cdd:cd10532    174 FNVFIDnldtRLPRIALFSTRTIKAGEELTFDYQMkgsgDLSSDsidnspakkRVRTVCKCGAVTCRGYL 243
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
252-330 8.46e-15

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: 73.21  E-value: 8.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  252 HQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCA-AAAGTFQDFRKltLLCPKH 330
Cdd:cd15664     28 HINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCArKAECVFQDDKK--VFCPAH 105
PHD_RSF1 cd15543
PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...
994-1038 3.95e-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: 69.22  E-value: 3.95e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15543      2 CRKCGLSDHPEWILLCDRCDAGYHTACLRPPLMIIPDGNWFCPPC 46
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
251-330 5.60e-14

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


Pssm-ID: 277170  Cd Length: 104  Bit Score: 70.68  E-value: 5.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  251 AHQRCAVWSRGVCRGEGtSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFRKLTLLCPKH 330
Cdd:cd15700     26 VHEACAVWTTGVYLVAG-KLFGLQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEENFSLRCPKH 104
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
4511-4592 5.95e-14

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: 70.33  E-value: 5.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4511 DLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTNVYHFTCAlKAQCTFFKDKT--ML 4588
Cdd:cd15695      8 ECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCA-AASGSFQSMKTllLL 86

                   ....
gi 1658251387 4589 CHAH 4592
Cdd:cd15695     87 CPEH 90
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
4846-4995 6.36e-14

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: 74.58  E-value: 6.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4846 KSSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKmyesqnrGVYMFRIDSE----H 4921
Cdd:cd10535     78 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 150
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4922 VIDATITGGPARYINHSCAPNCVAEVVTFE----KGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKI-PCHCGAVNCR 4995
Cdd:cd10535    151 CIDARFYGNVSRFINHHCEPNLVPVRVFMAhqdlRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 229
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
4511-4592 6.49e-14

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


Pssm-ID: 277166  Cd Length: 90  Bit Score: 70.36  E-value: 6.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4511 DLWVHLNCALWSTEVYETQAGALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTNVYHFTCALKAQcTF--FKDKTML 4588
Cdd:cd15696      8 ECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAG-TFqdFSRRLLL 86

                   ....
gi 1658251387 4589 CHAH 4592
Cdd:cd15696     87 CPTH 90
PHD2_KMT2C cd15594
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
993-1038 6.98e-14

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: 68.43  E-value: 6.98e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15594      1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
4869-4998 7.71e-14

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: 74.93  E-value: 7.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4869 QGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNrGVYMFRID---SEHVIDATITGGPARYINHSCAPNCVA 4945
Cdd:cd10525     97 RGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQV 175
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4946 EVVTF----EKGHKIIISSNRKIQRGEELCYDYKF-----DLEDDQH-----------------KIPCHCGAVNCRKWM 4998
Cdd:cd10525    176 YNVFIdnldERLPRIALFATRTIRAGEELTFDYNMqvdpvDAESTKMdsnfglaglpgspkkrvRIECKCGVRSCRKYL 254
PHD_BAZ1A cd15627
PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...
391-435 1.12e-13

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: 67.80  E-value: 1.12e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15627      2 CRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC 46
PHD1_KDM5A cd15602
PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...
993-1040 1.66e-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: 67.67  E-value: 1.66e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCVS 1040
Cdd:cd15602      1 VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVA 48
PHD_BAZ1A cd15627
PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...
994-1038 1.98e-13

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: 67.42  E-value: 1.98e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15627      2 CRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC 46
PHD1_Lid_like cd15605
PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...
993-1038 2.14e-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: 67.09  E-value: 2.14e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15605      1 VCHTCGRGDGEESMLLCDGCDDSYHTFCLLPPLSEVPKGDWRCPKC 46
PHD2_KMT2C_like cd15510
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
993-1038 4.33e-13

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: 66.30  E-value: 4.33e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15510      1 VCQACRQPGDDTKMLVCETCDKGYHTSCLRPVMSSIPKYGWKCKNC 46
PHD_BAZ2A_like cd15545
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...
391-435 6.20e-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: 65.80  E-value: 6.20e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15545      2 CQICRSGDNEDQLLLCDGCDRGYHTYCFKPKMTNVPEGDWFCPEC 46
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
993-1041 7.45e-13

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: 65.98  E-value: 7.45e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQT--VPKGSWKCKWCVSC 1041
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPaeIPSGEWLCPECKPK 51
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
4872-4977 8.79e-13

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: 68.07  E-value: 8.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4872 GLYAARDIEKYTMVIEYIGTI-IRNEV--ANRKEKMYESqnrgvYMFRIDSEH----VIDATITGGPARYINHSCAPNCV 4944
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEVsLRSEFkeDNGFFKRPSP-----FVFFYDGFEglplCVDARKYGNEARFIRRSCRPNAE 92
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1658251387 4945 AEVVTFEKG-HKIIISSNRKIQRGEELCYDYKFD 4977
Cdd:cd10529     93 LRHVVVSNGeLRLFIFALKDIRKGTEITIPFDYD 126
PHD_BAZ1A_like cd15544
PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...
994-1038 1.03e-12

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: 65.12  E-value: 1.03e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15544      2 CKVCRKKGDPDNMILCDGCDKAFHLYCLRPALREVPSGDWFCPAC 46
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
4488-4592 1.03e-12

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: 67.25  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGD----GLTDGPArllnldLDLWVHLNCALWSTEVYETqAGALINVELALRRGLSIRCVYCQRTGATSGCHRL 4563
Cdd:cd15699      1 CCLCGKWANyrnlGDLFGPF------YEFWVHEGCILWANGIYLV-CGRLYGLQEALDIAREMKCSHCQEAGATLGCYNK 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 1658251387 4564 RCTNVYHFTCALKAQCTFFKDK-TMLCHAH 4592
Cdd:cd15699     74 GCSFRYHYPCAIDADCLLNEENfSVRCPKH 103
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
4870-4996 1.19e-12

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: 71.94  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMY--------------ESQNRGvymFRIDSE---HVIDATITGGPA 4932
Cdd:cd10517    140 GWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYgdeyfaeldyievvEKLKEG---YESDVEehcYIIDAKSEGNLG 216
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4933 RYINHSCAPNCVAEVVtFEKGHKIIIS-----SNRKIQRGEELCYDYKFDLEDDQHKI-PCHCGAVNCRK 4996
Cdd:cd10517    217 RYLNHSCSPNLFVQNV-FVDTHDLRFPwvaffASRYIRAGTELTWDYNYEVGSVPGKVlYCYCGSSNCRG 285
PHD1_KDM5C_5D cd15604
PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...
993-1038 1.37e-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: 1.37e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15604      1 VCRMCSRGDEDDKLLLCDGCDDNYHTFCLLPPLPEPPKGIWRCPKC 46
PHA03247 PHA03247
large tegument protein UL36; Provisional
2013-2574 1.43e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 74.97  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2013 PDTPRP---------AVTADPFVKPMGPPKAGIVLESQ--------GRHMPAS-VIGDAFarPSHraEAYQRMSHNKMvl 2074
Cdd:PHA03247  2415 PDPPGPpdvrfvgseEIEELPFVSPGGDVLAGLAADGDpffartilGAPFSLSlLLGELF--PGA--PVYRRPAEARF-- 2488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2075 sdPYSkPLLTPIPGSnesGSVPLFKAPMPPPHPqdlynsTPSIGRRNSVDSFERPTRLS-----DTFSQNSQNDPyaHPP 2149
Cdd:PHA03247  2489 --PFA-AGAAPDPGG---GGPPDPDAPPAPSRL------APAILPDEPVGEPVHPRMLTwirglEELASDDAGDP--PPP 2554
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2150 LTPctsmnDNFSNSPKMMHHPQSNAFCQPMPMVRHPSRDAFAQASSTSRSDFTQKSPDPYTQPPGTPRPSDPYAQPPGTP 2229
Cdd:PHA03247  2555 LPP-----AAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPP 2629
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2230 RPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYS--PQQPSNRRSSPS----------HAMEPYPQ 2297
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASspPQRPRRRAARPTvgsltsladpPPPPPTPE 2709
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2298 P------PGTPCP-GTGERFSKSPVSQ-----RNADSYFQQPETPRLVKNDTYAQQPNIPKPVLSDPYSQPPGTPRPGVG 2365
Cdd:PHA03247  2710 PaphalvSATPLPpGPAAARQASPALPaapapPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2366 PEVFNRPVArtgPVSQDPFSSPQVTMQENFVRPQTPKHSGlsddgfaqPQSNPASQTPVHDPYAQAPMTPRPQLGDRLA- 2444
Cdd:PHA03247  2790 SLSESRESL---PSPWDPADPPAAVLAPAAALPPAASPAG--------PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAp 2858
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2445 -----REVKDQVEVGHEGSSHGVGQFSNLQQSTSNSTESQSGAQLPLgdteeklrqrQRLRELILRQQQQKSAIRQEKGL 2519
Cdd:PHA03247  2859 ggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQP----------ERPPQPQAPPPPQPQPQPPPPPQ 2928
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 2520 QEPSSSIPGTPRQwsqeetgqqnelfnrPPPPYPGTARGSVISTGQRFP---GLFPGE 2574
Cdd:PHA03247  2929 PQPPPPPPPRPQP---------------PLAPTTDPAGAGEPSGAVPQPwlgALVPGR 2971
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
390-438 1.63e-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: 64.82  E-value: 1.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDS--IPTNGWRCKNCRVC 438
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPaeIPSGEWLCPECKPK 51
PHD2_KMT2D cd15595
PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
993-1038 2.04e-12

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: 64.63  E-value: 2.04e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15595      1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
4486-4592 2.29e-12

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 66.21  E-value: 2.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4486 RKCCFCHEEGDGL---TDGparllnldldLWVHLNCALWSTEVY--ETQAGALINVELALRRGLSIRCVYC-QRTGATSG 4559
Cdd:pfam13832    1 VRCCLCPLRGGALkqtSDG----------RWVHVLCAIFVPEVRfgNVATMEPIDVSRIPPERWKLKCVFCkKRSGACIQ 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1658251387 4560 CHRLRCTNVYHFTCALKAQCTF------FKDKTMLCHAH 4592
Cdd:pfam13832   71 CSKGRCTTAFHVTCAQAAGVYMepedwpNVVVIAYCQKH 109
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
252-330 3.15e-12

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: 65.84  E-value: 3.15e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387  252 HQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQdFRKLTLLCPKH 330
Cdd:cd15698     28 HLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIRAKCMF-FKDKTMLCPMH 105
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
4488-4592 3.24e-12

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: 65.67  E-value: 3.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEegdgltdgPARLLNL-DL------DLWVHLNCALWSTEVYETqAGALINVELALRRGLSIRCVYCQRTGATSGC 4560
Cdd:cd15700      1 CCLCRN--------PANYKDLgDLcgpyypEHWVHEACAVWTTGVYLV-AGKLFGLQEAVQKAADAKCSSCQGAGATVGC 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1658251387 4561 HRLRCTNVYHFTCALKAQCTFFKDK-TMLCHAH 4592
Cdd:cd15700     72 CHKGCTQSYHYICAVEAGCLFEEENfSLRCPKH 104
PHD_UHRF1_2 cd15525
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...
994-1038 3.34e-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: 63.93  E-value: 3.34e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGS-WKCKWC 1038
Cdd:cd15525      2 CHVCGGKQDPEKQLLCDECDMAYHLYCLDPPLTSLPDDDeWYCPDC 47
PHD_PHRF1 cd15536
PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also ...
994-1038 3.45e-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: 63.59  E-value: 3.45e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15536      2 CEVCGRSDREDRLLLCDGCDAGYHMECLTPPLDEVPIEEWFCPEC 46
PHD5_KMT2C_like cd15513
PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...
390-435 4.11e-12

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: 63.65  E-value: 4.11e-12
                           10        20        30        40
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gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15513      1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 46
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
252-330 4.20e-12

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: 65.45  E-value: 4.20e-12
                           10        20        30        40        50        60        70        80
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gi 1658251387  252 HQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAG-TFqdFRKLTLLCPKH 330
Cdd:cd15697     28 HLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAIKAQcMF--FKDKTMLCPMH 105
PHD_UHRF1 cd15616
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); ...
994-1038 4.23e-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: 63.45  E-value: 4.23e-12
                           10        20        30        40
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gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVP-KGSWKCKWC 1038
Cdd:cd15616      2 CHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPdDEDWYCPEC 47
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
390-435 4.31e-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: 63.48  E-value: 4.31e-12
                           10        20        30        40
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gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQpvMDSIPTNGWRCKNC 435
Cdd:cd15529      1 TCTKCGDPHDEDKMMFCDQCDRGYHTFCVG--LRSIPDGRWICPLC 44
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
4846-4995 4.33e-12

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: 69.28  E-value: 4.33e-12
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gi 1658251387 4846 KSSQYRKMKTEWKTNVYLARSRIQGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKmyesqnrGVYMFRIDSE----H 4921
Cdd:cd10533     78 RNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 150
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4922 VIDATITGGPARYINHSCAPNCVAEVVTFE----KGHKIIISSNRKIQRGEELCYDYKFDLEDDQHK-IPCHCGAVNCR 4995
Cdd:cd10533    151 CIDARYYGNISRFINHLCDPNIIPVRVFMLhqdlRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 229
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
252-330 4.97e-12

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: 65.45  E-value: 4.97e-12
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gi 1658251387  252 HQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAA-GTFQDFRKltLLCPKH 330
Cdd:cd15694     28 HVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCARASrCCFQDDKK--VFCQKH 105
PHD_RSF1 cd15543
PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...
388-435 5.74e-12

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: 63.06  E-value: 5.74e-12
                           10        20        30        40
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gi 1658251387  388 CKVCQTCKNPgedSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15543      2 CRKCGLSDHP---EWILLCDRCDAGYHTACLRPPLMIIPDGNWFCPPC 46
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
250-330 6.24e-12

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: 65.35  E-value: 6.24e-12
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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  250 CAHQRCAVWSRGVC-RGEGTSLLN------VDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGT----FQ 318
Cdd:cd15669     24 CAHYFCLLFSSGLPqRGEDNEGIYgflpedIRKEVRRASRLRCFYCKKKGASIGCAVKGCRRSFHFPCGLENGCvtqfFG 103
                           90
                   ....*....|..
gi 1658251387  319 DFRKltlLCPKH 330
Cdd:cd15669    104 EYRS---FCWEH 112
PHD3_KMT2C cd15511
PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
469-519 8.48e-12

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: 62.89  E-value: 8.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  469 CPLCGKPLGAEFLSDHLTCQSCKRYLHLECERQAGGRTDPLDREGYICTLC 519
Cdd:cd15511      2 CPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52
PHD2_d4 cd15530
PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three ...
994-1038 1.18e-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: 62.40  E-value: 1.18e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15530      2 CSLCGTSENDDQLLFCDDCDRGYHMYCLSPPMSEPPEGSWSCHLC 46
PHD1_KDM5A_like cd15515
PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...
390-435 1.59e-11

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: 62.02  E-value: 1.59e-11
                           10        20        30        40
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gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15515      1 ICQVCGRGDDEDKLLLCDGCDDSYHTFCLIPPLPDIPPGDWRCPKC 46
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
242-330 1.73e-11

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


Pssm-ID: 277169  Cd Length: 103  Bit Score: 63.78  E-value: 1.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  242 LFDPTGQCCAHQRCAVWSRGVCRGEGtSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDFR 321
Cdd:cd15699     16 LFGPFYEFWVHEGCILWANGIYLVCG-RLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLNEE 94

                   ....*....
gi 1658251387  322 KLTLLCPKH 330
Cdd:cd15699     95 NFSVRCPKH 103
PHD_BAZ1A_like cd15544
PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...
391-435 1.80e-11

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: 61.66  E-value: 1.80e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15544      2 CKVCRKKGDPDNMILCDGCDKAFHLYCLRPALREVPSGDWFCPAC 46
PHD1_KDM5C_5D cd15604
PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...
390-435 3.58e-11

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: 61.01  E-value: 3.58e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15604      1 VCRMCSRGDEDDKLLLCDGCDDNYHTFCLLPPLPEPPKGIWRCPKC 46
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
993-1038 4.48e-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: 60.69  E-value: 4.48e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1658251387   993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQT-VPKGSWKCKWC 1038
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
251-333 5.35e-11

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: 62.71  E-value: 5.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  251 AHQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAG-TFQDFRKltLLCPK 329
Cdd:cd15693     29 THVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNcVFLEDKK--VYCQR 106

                   ....
gi 1658251387  330 HIEL 333
Cdd:cd15693    107 HKDL 110
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
4488-4592 6.06e-11

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


Pssm-ID: 277143  Cd Length: 116  Bit Score: 62.41  E-value: 6.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGParLLNLDLDLWVHLNCALWSTEVYETQ-------AGALIN-VELALRRGLSIRCVYCQRTGATSG 4559
Cdd:cd15673      1 CGFCKSGEENKETGG--KLASGEKIAAHHNCMLFSSGLVQYVspnendfGGFDIEdVKKEIKRGRKLKCNLCKKTGATIG 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1658251387 4560 CHRLRCTNVYHFTCALKAQCTFFKDK-----TMLCHAH 4592
Cdd:cd15673     79 CDVKQCKKTYHYHCAKKDDAKIIERNsqgiyRVYCKNH 116
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
390-435 7.45e-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: 59.92  E-value: 7.45e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1658251387   390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDS-IPTNGWRCKNC 435
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
4870-4974 7.60e-11

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


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 62.40  E-value: 7.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4870 GLGLYAARDIEKytmvieyiGTIIRNE------VANRKEKMYESQNRGVYMFRIdsehvidatitggpARYINHSCAPNC 4943
Cdd:cd20071     10 GRGLVATRDIEP--------GELILVEkplvsvPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA 67
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1658251387 4944 VaevVTFEKGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd20071     68 V---VVFDGNGTLRVRALRDIKAGEELTISY 95
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
4869-4996 7.83e-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: 65.64  E-value: 7.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4869 QGLGLYAARDIEKYTMVIEYIGTIIRNEVANRKEKMYESQNRGVYMFRIDSEHVIDATITGGPARYINHSCAPNCVAEVV 4948
Cdd:cd10541    102 KGWGIRCLDDIAKGTFVCIYAGKILTDDFADKEGLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNV 181
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 4949 tFEKGHK-----IIISSNRKIQRGEELCYDYKFDLED-DQHKIPCHCGAVNCRK 4996
Cdd:cd10541    182 -FVDTHDlrfpwVAFFASKRIKAGTELTWDYNYEVGSvEGKELLCCCGSNECRG 234
PHD_UHRF2 cd15617
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...
994-1038 9.01e-11

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: 59.97  E-value: 9.01e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGS-WKCKWC 1038
Cdd:cd15617      2 CYVCGGKQDAHMQLLCDECNMAYHIYCLNPPLDKIPEDEdWYCPSC 47
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
994-1038 1.03e-10

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: 59.70  E-value: 1.03e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15527      2 CSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
4871-4985 1.05e-10

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: 63.58  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4871 LGLYAARDIEKYTMVIEYIGTI-IRNEVANRKEKMYE---SQNRGVYmFRIDSEHVIDATITGGPARYINHSCAPNCVAE 4946
Cdd:cd19183     14 FGLFADRPIPAGDPIQELLGEIgLQSEYIADPENQYQilgAPKPHVF-FHPQSPLYIDTRRSGSVARFIRRSCRPNAELV 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1658251387 4947 VVTFEKGH--KIIISSNRKIQRGEELCYDYKFDLEDDQHKI 4985
Cdd:cd19183     93 TVASDSGSvlKFVLYASRDISPGEEITIGWDWDNPHPFRRF 133
PHD_BAZ1B cd15628
PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...
391-435 1.16e-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: 59.37  E-value: 1.16e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15628      2 CKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC 46
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
4869-4998 1.36e-10

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: 65.24  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4869 QGLGLYAARDIEKYTMVIEYIGTIIRNEV------ANRKEKMYESQNRGVYMFRI--------DSEHVIDATITGGPARY 4934
Cdd:cd10523    118 KGWGVRCLDDIDKGTFVCIYAGRVLSRARspteplPPKLELPSENEVEVVTSWLIlskkrklrENVCFLDASKEGNVGRF 197
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4935 INHSCAPNCVAEVVTFEKGHK----IIISSNRKIQRGEELCYDYKFDLEDDQHK-IPCHCGAVNCRKWM 4998
Cdd:cd10523    198 LNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYSYDAGTSPEQeIPCLCGVNKCQKKI 266
PHD_BAZ2A_like cd15545
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...
994-1038 1.45e-10

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: 59.25  E-value: 1.45e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15545      2 CQICRSGDNEDQLLLCDGCDRGYHTYCFKPKMTNVPEGDWFCPEC 46
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
944-994 1.62e-10

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 59.04  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  944 CVVCGsfGQGAEGRLLACSQCGQCYHPYCVNIKITRVVLSKG-WRCLECTVC 994
Cdd:pfam00628    2 CAVCG--KSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1957-2366 1.90e-10

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 67.89  E-value: 1.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1957 TPRPPPIGSSTPRRNSTESCSAPRLPSEQQERGRPSSGHESFGSPTSASVDPYAKPPDTPRPAVTADPFVKPMGPP-KAG 2035
Cdd:PHA03307    62 CDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlRPV 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2036 IVLESQGRHMPASVIGDAFARPSHRAEAYQrmshnkmvLSDPYSKPLLTPIPGSNESGSVPLFKAPMPPPHPQDLYNSTP 2115
Cdd:PHA03307   142 GSPGPPPAASPPAAGASPAAVASDAASSRQ--------AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPI 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2116 SIGRRNSVDSFERptrlSDTFSQNSQNDPYAHPPLTPCTSMNDNFSNSPkmmhhpqsnafcqPMPMVRHPSRDAFAQASS 2195
Cdd:PHA03307   214 SASASSPAPAPGR----SAADDAGASSSDSSSSESSGCGWGPENECPLP-------------RPAPITLPTRIWEASGWN 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2196 TSRSDFTQKSPDPYTQPP-GTPRPSDPYAQPPGTPRPAYDPYAQPP----GTPRPFDPYSKPPGTPRPASDSFSNSASRP 2270
Cdd:PHA03307   277 GPSSRPGPASSSSSPRERsPSPSPSSPGSGPAPSSPRASSSSSSSResssSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2271 GGvdqySPQQPSNRRSSPSHAMEPYP-QPPGTPCPGTGERFSKSPVSQRNADSYF-QQPETPRLVKNDTYAQQPNIPKPV 2348
Cdd:PHA03307   357 PP----PADPSSPRKRPRPSRAPSSPaASAGRPTRRRARAAVAGRARRRDATGRFpAGRPRPSPLDAGAASGAFYARYPL 432
                          410
                   ....*....|....*...
gi 1658251387 2349 LSdpysqPPGTPRPGVGP 2366
Cdd:PHA03307   433 LT-----PSGEPWPGSPP 445
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
4488-4592 2.50e-10

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: 60.73  E-value: 2.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGlTDGPARLLNLDlDLWVHLNCALWSTEVYETQ------AGALIN-VELALRRGLSIRCVYCQRTGATSGC 4560
Cdd:cd15669      1 CVLCGRSDDD-PDKYGEKLQKD-GICAHYFCLLFSSGLPQRGednegiYGFLPEdIRKEVRRASRLRCFYCKKKGASIGC 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1658251387 4561 HRLRCTNVYHFTCALKAQCT--FFKDKTMLCHAH 4592
Cdd:cd15669     79 AVKGCRRSFHFPCGLENGCVtqFFGEYRSFCWEH 112
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
991-1038 3.06e-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: 58.06  E-value: 3.06e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  991 CTVCeacgqaSDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15532      2 CRVC------KDGGELLCCDGCPSSYHLHCLNPPLAEIPDGDWFCPRC 43
PHD1_Lid_like cd15605
PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...
390-435 3.36e-10

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: 58.23  E-value: 3.36e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15605      1 VCHTCGRGDGEESMLLCDGCDDSYHTFCLLPPLSEVPKGDWRCPKC 46
PHD_BAZ2A cd15629
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); BAZ2A, also ...
391-435 3.42e-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: 58.32  E-value: 3.42e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15629      2 CLVCRKGDNDEYLLLCDGCDRGCHMYCHRPKMLQVPEGDWFCPNC 46
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
993-1038 3.82e-10

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: 57.70  E-value: 3.82e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDppLQTVPKGSWKCKWC 1038
Cdd:cd15529      1 TCTKCGDPHDEDKMMFCDQCDRGYHTFCVG--LRSIPDGRWICPLC 44
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
943-991 4.12e-10

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 57.99  E-value: 4.12e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1658251387   943 MCVVCGSFGqgAEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLEC 991
Cdd:smart00249    1 YCSVCGKPD--DGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1899-2303 5.04e-10

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 66.35  E-value: 5.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1899 DDVFLRPQPPPPTGTrlteACSQGQASQPQSPQMFSTGTASSSSRPSSPWDPyakMVGTPRPPPigsSTPRRNSTESCSA 1978
Cdd:PHA03307    62 CDRFEPPTGPPPGPG----TEAPANESRSTPTWSLSTLAPASPAREGSPTPP---GPSSPDPPP---PTPPPASPPPSPA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1979 PRLPSEQqeRGRPSSGHESFGSPTSASVDPYAKPPDTPRPAVTADPF------VKPMGPPKAGIVLESQGRHMPASvigd 2052
Cdd:PHA03307   132 PDLSEML--RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLsspeetARAPSSPPAEPPPSTPPAAASPR---- 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2053 afARPSHRAEAYQRMSHN----KMVLSDPYSKPLLTPIPGSNESGSVPLFKAPMPPPHPQDLynstPSIGRRNSVDSfER 2128
Cdd:PHA03307   206 --PPRRSSPISASASSPApapgRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITL----PTRIWEASGWN-GP 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2129 PTRLSDTFSQNSQNDPYAHPpltpctsmndnfsnSPKmmhHPQSNAFCQPMPMVRHPSRDAFAQASSTSRSDFTQKSPDP 2208
Cdd:PHA03307   279 SSRPGPASSSSSPRERSPSP--------------SPS---SPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAV 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2209 YTQPPGT--PRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTpRPASDSFSNSASRPGGVDQySPQQPSNRRS 2286
Cdd:PHA03307   342 SPGPSPSrsPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA-RAAVAGRARRRDATGRFPA-GRPRPSPLDA 419
                          410
                   ....*....|....*..
gi 1658251387 2287 SPSHAMEPYPQPPGTPC 2303
Cdd:PHA03307   420 GAASGAFYARYPLLTPS 436
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
344-391 5.15e-10

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 57.89  E-value: 5.15e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  344 CAVCDSPGDLLDQLFCTTCGQHYHGTCLDIGVT--PLKRAGWQCPECKVC 391
Cdd:pfam00628    2 CAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDpaEIPSGEWLCPECKPK 51
PHD1_Lid2p_like cd15519
PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...
388-435 5.20e-10

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: 57.48  E-value: 5.20e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  388 CKVCQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15519      2 CEVCGLDDNEGE---VLLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC 46
PRK10263 PRK10263
DNA translocase FtsK; Provisional
2205-2754 6.29e-10

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 66.26  E-value: 6.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2205 SPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQ--------- 2275
Cdd:PRK10263   376 APEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAwqaeeqqst 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2276 YSPQ---QPSNRRSSPSHAMEPYPQPPGTPCPGTGErfsKSPVSQRNADS-----YFQQPETPRLVKNDTYAQ--QPnIP 2345
Cdd:PRK10263   456 FAPQstyQTEQTYQQPAAQEPLYQQPQPVEQQPVVE---PEPVVEETKPArpplyYFEEVEEKRAREREQLAAwyQP-IP 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2346 KPVlSDPYSQPPGTPRPGVGPEVFNRPVARTGPVSQdpfSSPQVTMqenfvrpqtpkHSGlSDDGFAQPQSNPASQTpvh 2425
Cdd:PRK10263   532 EPV-KEPEPIKSSLKAPSVAAVPPVEAAAAVSPLAS---GVKKATL-----------ATG-AAATVAAPVFSLANSG--- 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2426 dpyaqapmTPRPQ----LGDRLAREVKDQVEVGHEGSSHGVG----QFSNLQQSTSNSTESQSGAQLPLGDTEEkLRQRQ 2497
Cdd:PRK10263   593 --------GPRPQvkegIGPQLPRPKRIRVPTRRELASYGIKlpsqRAAEEKAREAQRNQYDSGDQYNDDEIDA-MQQDE 663
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2498 RLRELILRQQQQKSAIRQEKglqepsssipgTPRQWSQEETGQQNELfnrppppypgtARGSVISTGQRFPGLFPGeqrG 2577
Cdd:PRK10263   664 LARQFAQTQQQRYGEQYQHD-----------VPVNAEDADAAAEAEL-----------ARQFAQTQQQRYSGEQPA---G 718
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2578 AfqNEGQFPRAQFSADVANMGMRPPEPRFGfPSGGQVTLGGQGHFLRSPHHMQGPMIDVPQQMRRslsvdlsrtignnsl 2657
Cdd:PRK10263   719 A--NPFSLDDFEFSPMKALLDDGPHEPLFT-PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQ--------------- 780
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2658 llpqhfPPRSIPLQQHniMGQPFIELRHRAPENRVRLPFAPPAiagnvvdqsvQSQRPADPMLSQPsgitSHMQISSSME 2737
Cdd:PRK10263   781 ------PQQPVAPQPQ--YQQPQQPVAPQPQYQQPQQPVAPQP----------QYQQPQQPVAPQP----QYQQPQQPVA 838
                          570       580
                   ....*....|....*....|....
gi 1658251387 2738 NPHQQSL--PL-----NTEPQQAP 2754
Cdd:PRK10263   839 PQPQDTLlhPLlmrngDSRPLHKP 862
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
249-330 7.41e-10

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: 59.33  E-value: 7.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  249 CCAHQRCAVWSRG-VCRG-------EGTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCAAAAGTFQDF 320
Cdd:cd15673     23 IAAHHNCMLFSSGlVQYVspnendfGGFDIEDVKKEIKRGRKLKCNLCKKTGATIGCDVKQCKKTYHYHCAKKDDAKIIE 102
                           90
                   ....*....|....
gi 1658251387  321 RKLT----LLCPKH 330
Cdd:cd15673    103 RNSQgiyrVYCKNH 116
PHD_PHF21A cd15523
PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...
991-1038 9.15e-10

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: 56.64  E-value: 9.15e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  991 CTVCEACGQasdpgrLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15523      2 CSVCRKSGE------LLMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
390-435 9.25e-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: 56.91  E-value: 9.25e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15532      1 FCRVCKDGGE---LLCCDGCPSSYHLHCLNPPLAEIPDGDWFCPRC 43
PHD2_PHF14 cd15562
PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
993-1044 1.42e-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: 56.65  E-value: 1.42e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWcvSCTQC 1044
Cdd:cd15562      1 SCGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTRMPKKTKNSGW--QCSEC 50
PHD_BAZ1B cd15628
PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...
994-1038 2.03e-09

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: 55.91  E-value: 2.03e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15628      2 CKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC 46
PHD_PHRF1 cd15536
PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also ...
391-435 2.10e-09

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: 55.88  E-value: 2.10e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15536      2 CEVCGRSDREDRLLLCDGCDAGYHMECLTPPLDEVPIEEWFCPEC 46
PHD1_KDM5B cd15603
PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis ...
390-435 3.35e-09

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: 55.34  E-value: 3.35e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15603      1 VCLVCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC 46
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
994-1038 3.40e-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: 55.15  E-value: 3.40e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGqasDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15539      2 CAVCG---DGGELLCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43
PHD1_KDM5A cd15602
PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...
390-435 4.06e-09

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: 55.34  E-value: 4.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15602      1 VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKC 46
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
391-435 6.02e-09

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: 54.69  E-value: 6.02e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15527      2 CSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46
PHD_UHRF1_2 cd15525
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...
391-435 8.16e-09

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: 54.30  E-value: 8.16e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNG-WRCKNC 435
Cdd:cd15525      2 CHVCGGKQDPEKQLLCDECDMAYHLYCLDPPLTSLPDDDeWYCPDC 47
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
390-435 1.12e-08

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 53.86  E-value: 1.12e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  390 VCQTCKNPGED-SKMLVCDTCDKGYHTFCLQP-VMDSIPTNGWRCKNC 435
Cdd:cd15489      1 SCIVCGKGGDLgGELLQCDGCGKWFHADCLGPpLSSFVPNGKWICPVC 48
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
993-1038 1.29e-08

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 53.86  E-value: 1.29e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  993 VCEACGQASD-PGRLLLCDDCDISYHTYCLDPPLQT-VPKGSWKCKWC 1038
Cdd:cd15489      1 SCIVCGKGGDlGGELLQCDGCGKWFHADCLGPPLSSfVPNGKWICPVC 48
PHD1_PHF12 cd15533
PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...
993-1038 2.59e-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: 52.74  E-value: 2.59e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  993 VCEACGQAsdpGRLLLCDDCDISYHTYCLDPPL--QTVPKGSWKCKWC 1038
Cdd:cd15533      1 YCDSCGEG---GDLLCCDRCPASFHLQCCNPPLdeEDLPPGEWLCHRC 45
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
344-388 2.64e-08

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 52.98  E-value: 2.64e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1658251387   344 CAVCDSPGDLLDQLFCTTCGQHYHGTCLDI-GVTPLKRAGWQCPEC 388
Cdd:smart00249    2 CSVCGKPDDGGELLQCDGCDRWYHQTCLGPpLLEEEPDGKWYCPKC 47
PHD1_CHD_II cd15531
PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
994-1038 2.96e-08

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: 52.60  E-value: 2.96e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQAsdpGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15531      2 CEVCQQG---GEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHC 43
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
943-991 3.76e-08

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 52.32  E-value: 3.76e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1658251387  943 MCVVCGSFGQGaEGRLLACSQCGQCYHPYCVNIKITRVVLSKGWRCLEC 991
Cdd:cd15489      1 SCIVCGKGGDL-GGELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
251-330 4.29e-08

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 54.27  E-value: 4.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  251 AHQRCAVWSRGVCRGEGTSLLNVD--KAIDSGSTESCAYC-KRLGASIKCCQEECSRSYHYPCAAAAGTFQDFR-----K 322
Cdd:pfam13832   22 VHVLCAIFVPEVRFGNVATMEPIDvsRIPPERWKLKCVFCkKRSGACIQCSKGRCTTAFHVTCAQAAGVYMEPEdwpnvV 101

                   ....*...
gi 1658251387  323 LTLLCPKH 330
Cdd:pfam13832  102 VIAYCQKH 109
PHD2_d4 cd15530
PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three ...
388-435 4.37e-08

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: 52.00  E-value: 4.37e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  388 CKVCQTCKNpgeDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15530      2 CSLCGTSEN---DDQLLFCDDCDRGYHMYCLSPPMSEPPEGSWSCHLC 46
PHD_BAZ2A cd15629
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); BAZ2A, also ...
994-1039 4.93e-08

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: 52.16  E-value: 4.93e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCV 1039
Cdd:cd15629      2 CLVCRKGDNDEYLLLCDGCDRGCHMYCHRPKMLQVPEGDWFCPNCV 47
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
234-330 5.37e-08

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: 54.13  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  234 PDGTDVQSLFDPTGQ-CCAHQRCAVWSRGVCRGEGTSLLNVDKAIDSGSTES---------CAYCKRLGASIKCCQEECS 303
Cdd:cd15712      5 PKGEEYSIMYFAQEQnIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNeikrgkrlkCNFCRKKGATVGCEERACR 84
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1658251387  304 RSYHYPCA----AAAGTFQDFRKLTLLCPKH 330
Cdd:cd15712     85 RSYHYFCAlcddAAIETDEVRGIYRVFCQKH 115
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
391-435 9.11e-08

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: 51.30  E-value: 9.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15539      2 CAVCGDGGE---LLCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43
PHD3_PHF14 cd15563
PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
990-1038 1.02e-07

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: 1.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  990 ECTVCEACGQASDpgrLLLCDDCDISYHTYCLDPPLQTVPKG---SWKCKWC 1038
Cdd:cd15563      1 ECCVCKQTGDNSQ---LVRCDECKLCYHFGCLDPPLKKSPKQrgyGWVCEEC 49
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1861-2304 1.14e-07

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 58.63  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1861 SPMTPQP----TNGSTSPVQHMVPKDSLACSQLPGTPtsgslddvflrPQPPPPTGTRLTEACSQGQASQPQSPQMFSTG 1936
Cdd:pfam03154  145 SPSIPSPqdneSDSDSSAQQQILQTQPPVLQAQSGAA-----------SPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1937 TASSSSRPSSPWDPYAKMVGTPRPPPigsstprrnstescsaPRLPSEQqergrpssghesfgSPTSASVDPyaKPPDTP 2016
Cdd:pfam03154  214 TSQPPNQTQSTAAPHTLIQQTPTLHP----------------QRLPSPH--------------PPLQPMTQP--PPPSQV 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2017 RPAVTADPFVKPMGPPkAGIVLESQGRHMPASVIGDAFARPSHRAEAYQRMSHNKMVLSDPYSKPLLTPIPGSNESGS-- 2094
Cdd:pfam03154  262 SPQPLPQPSLHGQMPP-MPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQpp 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2095 --VPLFKAPMPPPHPQDlyNSTPSIGRRNSVDSFERPTRLS--DTFSQNSQNDPyaHPPLTPCTSMNDnfsnspkmmHHP 2170
Cdd:pfam03154  341 reQPLPPAPLSMPHIKP--PPTTPIPQLPNPQSHKHPPHLSgpSPFQMNSNLPP--PPALKPLSSLST---------HHP 407
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2171 QSnafCQPMPMVRHPSrdafaqasstsrsdfTQKSPDPYTQPPG---TPRPSDPYAQPPgTPRPAYDPYAQPPGTPRPFD 2247
Cdd:pfam03154  408 PS---AHPPPLQLMPQ---------------SQQLPPPPAQPPVltqSQSLPPPAASHP-PTSGLHQVPSQSPFPQHPFV 468
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387 2248 PYSKPPGTPrPASDSFSNSASRPGgvdqysPQQPSnrrSSPSHAMEPYPQPPGTPCP 2304
Cdd:pfam03154  469 PGGPPPITP-PSGPPTSTSSAMPG------IQPPS---SASVSSSGPVPAAVSCPLP 515
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
344-388 1.62e-07

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 50.78  E-value: 1.62e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  344 CAVCDSPGDLLDQ-LFCTTCGQHYHGTCLDIGVTPL-KRAGWQCPEC 388
Cdd:cd15489      2 CIVCGKGGDLGGElLQCDGCGKWFHADCLGPPLSSFvPNGKWICPVC 48
PHD_BAZ2B cd15630
PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also ...
994-1040 1.67e-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: 50.74  E-value: 1.67e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCVS 1040
Cdd:cd15630      3 CQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPEGDWFCPACIA 49
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
2145-2392 1.79e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 57.78  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2145 YAHPPLTPCTSMNDNFSNSPKMMHHPQSNAFCQPMPMVRHPSRDAFAQASSTSRSDFTQKSPDPYTQPPGTPRPSDP--- 2221
Cdd:PTZ00449   575 LSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPkii 654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2222 -YAQPPGTPRPAYDPYAQppgtPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRRSSPShamepyPQPPG 2300
Cdd:PTZ00449   655 kSPKPPKSPKPPFDPKFK----EKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPR------PLPPK 724
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2301 TPcpgTGERFSKSPVSQRNADS-----YFQQPETPRLVKNDTYAQQPniPKPVLSDPYSQPPGTPRPGVGPEVFNRPVAR 2375
Cdd:PTZ00449   725 LP---RDEEFPFEPIGDPDAEQpddieFFTPPEEERTFFHETPADTP--LPDILAEEFKEEDIHAETGEPDEAMKRPDSP 799
                          250
                   ....*....|....*..
gi 1658251387 2376 TGPVSQDPFSSPQVTMQ 2392
Cdd:PTZ00449   800 SEHEDKPPGDHPSLPKK 816
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
990-1038 1.97e-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: 1.97e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1658251387  990 ECTVCEacgqasDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15541      1 WCAVCQ------NGGELLCCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC 43
PHD1_Rco1 cd15535
PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...
994-1038 2.18e-07

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: 50.11  E-value: 2.18e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  994 CEACGQasdPGRLLLCDDCDISYHTYCLDPPL--QTVPKGSWKCKWC 1038
Cdd:cd15535      2 CSACGG---YGSFLCCDGCPRSFHFSCLDPPLeeDNLPDDEWFCNEC 45
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
3355-3633 2.26e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 57.33  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3355 QQPPMVAGMQPQTVMLSGG---PPINQPRMSPMMQMQPYHNQPNAPRMSGIPGWHPGAPRPIGPGVPAPMASQAPSANTV 3431
Cdd:pfam09606  173 QMGPNGGPGQGQAGGMNGGqqgPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQG 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3432 QPVQTANGGGAPHvKFDDNNPFSEGFQERERKERLREQQERQRVQLMQEVERQRALQQRMEMEQQGLLGPDGNQDTLSQM 3511
Cdd:pfam09606  253 QQSQLGMGINQMQ-QMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMN 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3512 AFYG-----TDLPRDFM---QPQRPSAPQQMFPQQGVQPSFMSSSPGTFFMQTGERRPLIGngsfsseMGPSFRPKHLML 3583
Cdd:pfam09606  332 QSVGqggqvVALGGLNHletWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF-------MRQSPQPSVPSP 404
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 3584 QGPSFGPGQPRPPGFT-GPGMMPQGSadgPPFGVESATPLPPNYPGSGQSL 3633
Cdd:pfam09606  405 QGPGSQPPQSHPGGMIpSPALIPSPS---PQMSQQPAQQRTIGQDSPGGSL 452
PHD_BAZ2B cd15630
PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also ...
391-435 2.47e-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: 49.97  E-value: 2.47e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15630      3 CQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPEGDWFCPAC 47
dnaA PRK14086
chromosomal replication initiator protein DnaA;
2207-2423 3.62e-07

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 56.76  E-value: 3.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2207 DPYTQPPGTPRPSDPYAQPPGTPRPA---YDPYAQPPGTPRP--FDPYSKPPgTPRPASDSFSNS---ASRPGGVDQYSP 2278
Cdd:PRK14086    89 DPSAGEPAPPPPHARRTSEPELPRPGrrpYEGYGGPRADDRPpgLPRQDQLP-TARPAYPAYQQRpepGAWPRAADDYGW 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2279 QQPSNRRSSPshamEPYPqPPGTPCPGTgERFSKSPVSQRNADSY-FQQPETPRlvkndtyaqqpnipkpvlsdPYSQPP 2357
Cdd:PRK14086   168 QQQRLGFPPR----APYA-SPASYAPEQ-ERDREPYDAGRPEYDQrRRDYDHPR--------------------PDWDRP 221
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 2358 G---TPRPGVGPEVFNRPvaRTGPVSQDPFSSPQVTmqenfVRPQTPKHSGlsddgfAQPQSNPASQTP 2423
Cdd:PRK14086   222 RrdrTDRPEPPPGAGHVH--RGGPGPPERDDAPVVP-----IRPSAPGPLA------AQPAPAPGPGEP 277
PHA03378 PHA03378
EBNA-3B; Provisional
2080-2440 4.30e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 56.61  E-value: 4.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2080 KPLLTPIPGSNESGSVPLFKAPMPP-PHPQDlynsTPSIGRRNSVDSFERPTRLSDTFSQNSQN----------DPYAHP 2148
Cdd:PHA03378   456 RPPTQPLEGPTGPLSVQAPLEPWQPlPHPQV----TPVILHQPPAQGVQAHGSMLDLLEKDDEDmeqrvmatllPPSPPQ 531
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2149 PLT----PC--TSMNDNFSNSPKMMH--HPQSNAFCQPMPMVRHPSRDAFAQASSTSRSDFTQKsPDPYTQPPGTPRPSD 2220
Cdd:PHA03378   532 PRAgrraPCvyTEDLDIESDEPASTEpvHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQT-PWPVPHPSQTPEPPT 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2221 PYAQPPGTPRPAYDPYAQPP-------GTPRPFDP--YSKPPGTPRPASDSFSNSASRPGGVD-QYSPQQPSNRR----- 2285
Cdd:PHA03378   611 TQSHIPETSAPRQWPMPLRPipmrplrMQPITFNVlvFPTPHQPPQVEITPYKPTWTQIGHIPyQPSPTGANTMLpiqwa 690
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2286 ----SSPSHAMEPYPQPPGTPCPGTGERFSKSPVSQRNADSYFQQPETPRLVKNDTYAQQPNIPKPVLSDPYSQPPG--- 2358
Cdd:PHA03378   691 pgtmQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPaaa 770
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2359 ------TPRPGVGPEVFNRPvaRTGPVSQDPFSSPQVTMQenFVRPQTPKHSGLSDDGFAQPQSN------PASQTPVHD 2426
Cdd:PHA03378   771 pgaptpQPPPQAPPAPQQRP--RGAPTPQPPPQAGPTSMQ--LMPRAAPGQQGPTKQILRQLLTGgvkrgrPSLKKPAAL 846
                          410
                   ....*....|....
gi 1658251387 2427 PyAQAPMTPRPQLG 2440
Cdd:PHA03378   847 E-RQAAAGPTPSPG 859
PHD1_CHD_II cd15531
PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
391-435 5.08e-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: 49.14  E-value: 5.08e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15531      2 CEVCQQGGE---IILCDTCPRAYHLVCLDPELEKAPEGKWSCPHC 43
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2189-2445 6.04e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 56.33  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2189 AFAQASSTSRSDFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSAS 2268
Cdd:PHA03307    99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2269 RPGGVDQYSPQQPSNRRSSPSHAMEPYPQPPG----------TPCPGTGERFSKSPVSQRNADSyfQQPETPRLVKNDTy 2338
Cdd:PHA03307   179 PEETARAPSSPPAEPPPSTPPAAASPRPPRRSspisasasspAPAPGRSAADDAGASSSDSSSS--ESSGCGWGPENEC- 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2339 aqqpnipkPVLSDPYSQPPGTPRPGVGPEVFNRPVARTGPVSQDPFSSPQVTMQENFVRPQTPKHSGLSDDGfAQPQSNP 2418
Cdd:PHA03307   256 --------PLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS-SSRESSS 326
                          250       260
                   ....*....|....*....|....*..
gi 1658251387 2419 ASQTPVHDPyAQAPMTPRPQLGDRLAR 2445
Cdd:PHA03307   327 SSTSSSSES-SRGAAVSPGPSPSRSPS 352
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
2204-2532 6.26e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 56.24  E-value: 6.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2204 KSPDPYTQPPGTPRPSDPyaQPPGTPRPAYDPyaQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQ----YSPQ 2279
Cdd:PTZ00449   565 KEHKPSKIPTLSKKPEFP--KDPKHPKDPEEP--KKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSpkrpPPPQ 640
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2280 QPSNRRSSPSHAMEPYPQPPGTPCPGTGERF--------------SKSPVSQRNADSYFQQ------PETPRLVKNDTYA 2339
Cdd:PTZ00449   641 RPSSPERPEGPKIIKSPKPPKSPKPPFDPKFkekfyddyldaaakSKETKTTVVLDESFESilketlPETPGTPFTTPRP 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2340 QQPNIPKpvlsDPYS--QPPGTP-RPGVGP-EVFNRPVARTGPVSQDPFSSPQV-TMQENFVRPQTPKHSGLSDDGFAQP 2414
Cdd:PTZ00449   721 LPPKLPR----DEEFpfEPIGDPdAEQPDDiEFFTPPEEERTFFHETPADTPLPdILAEEFKEEDIHAETGEPDEAMKRP 796
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2415 QS-NPASQTPVHDpYAQAPMTPRPQlgDRLAREVKDQVEVGHEGSSHGVGQFSNLQQSTSNSTesqsgaqlpLGDTEEKL 2493
Cdd:PTZ00449   797 DSpSEHEDKPPGD-HPSLPKKRHRL--DGLALSTTDLESDAGRIAKDASGKIVKLKRSKSFDD---------LTTVEEAE 864
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387 2494 RQRQRLRELIL--------------RQQQQKSAIRQEKGLQEPS----SSIPGTPRQ 2532
Cdd:PTZ00449   865 EMGAEARKIVVdddgteaddedthpPEEKHKSEVRRRRPPKKPSkpkkPSKPKKPKK 921
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
2204-2439 7.38e-07

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 55.70  E-value: 7.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2204 KSPDPYTQPPGTPRPSDPYAQ--PPG----TPRPaYDPYA-----QPPGTPRPFDPYSKPP------GTPRPASDSFSNS 2266
Cdd:PLN03209   337 DGPKPVPTKPVTPEAPSPPIEeePPQpkavVPRP-LSPYTayedlKPPTSPIPTPPSSSPAssksvdAVAKPAEPDVVPS 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2267 ASRPGGVDQYSPQQPSNRRSSPSHAMEPYP--QPPGTPCPgTGERFSKSPVSQRNADSyfQQPETPrlvkndtyaqqpni 2344
Cdd:PLN03209   416 PGSASNVPEVEPAQVEAKKTRPLSPYARYEdlKPPTSPSP-TAPTGVSPSVSSTSSVP--AVPDTA-------------- 478
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2345 PKPVLSDPYSQPPGTPRPGVGPEVFN--RPVARTGPVSQDPFSSPQVTMQENFVRPQTPKHSGLSDDGFAQPQSNPASQT 2422
Cdd:PLN03209   479 PATAATDAAAPPPANMRPLSPYAVYDdlKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPY 558
                          250
                   ....*....|....*..
gi 1658251387 2423 PVHDPYaQAPMTPRPQL 2439
Cdd:PLN03209   559 TMYEDL-KPPTSPTPSP 574
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2143-2620 8.31e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 8.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2143 DPYAHPPLTPCTSMNDNFSNSPKMMHHPQSNAFCQPMPMVRHPSRDAFAQASSTSRSDFTQKSPDPYTQPPGTPRPSDPy 2222
Cdd:PHA03307    19 EFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAP- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2223 AQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRRSSPSHAMEPypqPPGTP 2302
Cdd:PHA03307    98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASS---RQAAL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2303 CPGTGERFSKSPVSqrnadsyfqqPETPRLVKNDTYAQQPniPKPVLSDPYSQPPGTPRPGVGpevfnRPVARTGPVSQD 2382
Cdd:PHA03307   175 PLSSPEETARAPSS----------PPAEPPPSTPPAAASP--RPPRRSSPISASASSPAPAPG-----RSAADDAGASSS 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2383 PFSSPQVTMQENFVRPQTPKHSGLSDDGFAQPQSNPASQTPVHDPYAQAPMTPRPQLGDRLAREVKDQVEV--GHEGSSH 2460
Cdd:PHA03307   238 DSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPApsSPRASSS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2461 GVGQFSNLQQSTSNSTESQSGAQLPLGDTEEKLRQRQRLRElilrqqqqkSAIRQEKGLQEPSSSIPGTPRQWSQEETGQ 2540
Cdd:PHA03307   318 SSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP---------PADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2541 qnelfnrppppypgTARGSVISTGQRfpglfpgeQRGAFQNEGQFPRAQFSADVANMGMRPPEPRFGFPSG--------- 2611
Cdd:PHA03307   389 --------------RARAAVAGRARR--------RDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGepwpgsppp 446
                          490
                   ....*....|.
gi 1658251387 2612 --GQVTLGGQG 2620
Cdd:PHA03307   447 ppGRVRYGGLG 457
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
4511-4576 9.22e-07

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: 50.67  E-value: 9.22e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1658251387 4511 DLWVHLNCALWSTEVYETQAGALINVELA---------LRRGLSIRCVYCQRTGATSGCHRLRCTNVYHFTCALK 4576
Cdd:cd15712     20 NIAAHQNCLLYSSGFVESEEYNPLNLDRRfdvesvlneIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALC 94
HMG-box_SF cd00084
high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found ...
1685-1732 1.02e-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: 48.67  E-value: 1.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1685 LYTNMNFPNLKEEFPDWSTR--VKQIAKLWRKASSQERSPYVQKARDNRA 1732
Cdd:cd00084      8 LFSKEKRPKLKKENPDLSFTeiSKLLGERWKELSEEEKQPYEEKAKEDKE 57
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
240-311 1.29e-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: 50.34  E-value: 1.29e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387  240 QSLFDPTGQCCAHQRCAVWSRGVCRGE-------GTSLLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCA 311
Cdd:cd15710     14 QLLISENQKVAAHHKCMLFSSALVSSHsdsenlgGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCA 92
dnaA PRK14086
chromosomal replication initiator protein DnaA;
2099-2305 1.35e-06

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 54.83  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2099 KAPMPPPHPQDLYNSTPSIGRRNSVDSFERPtRLSDTFSQNSQNDPYAHPPLTpctsmndnfsnspkmmhHPQSNAFCQP 2178
Cdd:PRK14086    94 EPAPPPPHARRTSEPELPRPGRRPYEGYGGP-RADDRPPGLPRQDQLPTARPA-----------------YPAYQQRPEP 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2179 MPMVRhPSRDAFAQASstsRSDFTqkSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRP 2258
Cdd:PRK14086   156 GAWPR-AADDYGWQQQ---RLGFP--PRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRP 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387 2259 ASDSFSNSASRPGGVDQYSPQQPSNRRSSPSHAMEPyPQPPGTPCPG 2305
Cdd:PRK14086   230 EPPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLA-AQPAPAPGPG 275
PHD_UHRF1 cd15616
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); ...
391-435 2.66e-06

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


Pssm-ID: 277088  Cd Length: 47  Bit Score: 47.27  E-value: 2.66e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPT-NGWRCKNC 435
Cdd:cd15616      2 CHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPDdEDWYCPEC 47
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
2213-2446 2.96e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 53.62  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2213 PGTPRPsdPYAQPPGTPRPAYDPYAQPPGTPRPfdpysKPPGTPRPasdSFSNSASRPGgvDQYSPQQPSNRRSSPSHAM 2292
Cdd:NF033839   281 QDTPKE--PGNKKPSAPKPGMQPSPQPEKKEVK-----PEPETPKP---EVKPQLEKPK--PEVKPQPEKPKPEVKPQLE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2293 EPYPQ---PPGTPCPGTgerfskSPVSQRNADSYFQQPETPR-LVKNDTYAQQPNI-PKPVLSDPYSQP-PGTPRPGVGP 2366
Cdd:NF033839   349 TPKPEvkpQPEKPKPEV------KPQPEKPKPEVKPQPETPKpEVKPQPEKPKPEVkPQPEKPKPEVKPqPEKPKPEVKP 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2367 EVFN-RPVARTGPVSQDPFSSPQVTMQENFVRPQ--TPKHSGLSDDGFAQPQSNPASQTPVHDPYAQAPMTPRPQLGDRL 2443
Cdd:NF033839   423 QPEKpKPEVKPQPEKPKPEVKPQPEKPKPEVKPQpeTPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNL 502

                   ...
gi 1658251387 2444 ARE 2446
Cdd:NF033839   503 SKD 505
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
2212-2438 3.16e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.93  E-value: 3.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2212 PPGTPRPSDPYAQPPGTPRPAYDPYAQP------PGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRR 2285
Cdd:PTZ00449   497 APIEEEDSDKHDEPPEGPEASGLPPKAPgdkegeEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLS 576
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2286 SSPSHAMEP-YPQPPGTPcpgtgeRFSKSPVSQRNADSYfQQPETPRLVKNDTYAQQPNIPKPVLSDPYSQPPGTPRpgv 2364
Cdd:PTZ00449   577 KKPEFPKDPkHPKDPEEP------KKPKRPRSAQRPTRP-KSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPE--- 646
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2365 gpevfnRPVARTGPVSQDPFSSPQVTMQENF------------VRPQTPKHSGLSDDGFAQPQSNPASQTPVHDPYAQAP 2432
Cdd:PTZ00449   647 ------RPEGPKIIKSPKPPKSPKPPFDPKFkekfyddyldaaAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRP 720

                   ....*..
gi 1658251387 2433 MTP-RPQ 2438
Cdd:PTZ00449   721 LPPkLPR 727
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2212-2393 3.43e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.84  E-value: 3.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2212 PPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRRSSPSHA 2291
Cdd:PRK07764   602 APASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAP 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2292 ME---------PYPQPPGTPCPGTGERFSKSPVSQRNADSYfQQPETPRLVKNDTYAQQPNIPKPVLSDPYSQPPGTPRP 2362
Cdd:PRK07764   682 PPapapaapaaPAGAAPAQPAPAPAATPPAGQADDPAAQPP-QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1658251387 2363 GVGPEVFNRPVARTGPVSQDPfssPQVTMQE 2393
Cdd:PRK07764   761 PPAPAPAAAPAAAPPPSPPSE---EEEMAED 788
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2075-2425 3.63e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.62  E-value: 3.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2075 SDPYSKPLLTPIPGSNESGSVPLFKAPMPPPHPqdlynSTPSIGRRNSVDSFERP-TRLSDTFSQNSQNDPYAHPPLTPC 2153
Cdd:pfam03154  178 SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQG-----SPATSQPPNQTQSTAAPhTLIQQTPTLHPQRLPSPHPPLQPM 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2154 TSMNDNFSNSPKMMHHPQSNAFCQPMP--------MVRHP-SRDAFAQASSTSRSdftQKSPDPYTQPPGTP--RPSDPY 2222
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQPSLHGQMPPMPhslqtgpsHMQHPvPPQPFPLTPQSSQS---QVPPGPSPAAPGQSqqRIHTPP 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2223 AQPpgTPRPAYDPYAQP-PGTPRPFDPYSKPPGTPRPASDSfSNSASRPGGVDQYSP-QQPSNRRSSPshAMEPYPQPPG 2300
Cdd:pfam03154  330 SQS--QLQSQQPPREQPlPPAPLSMPHIKPPPTTPIPQLPN-PQSHKHPPHLSGPSPfQMNSNLPPPP--ALKPLSSLST 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2301 TPCPGtgerfSKSPVSQRNADSyfqQPETPRLVKNDTYAQQPNIPKPVLSDPysqPPGTPRPGVGPEVF-NRPVARTGPV 2379
Cdd:pfam03154  405 HHPPS-----AHPPPLQLMPQS---QQLPPPPAQPPVLTQSQSLPPPAASHP---PTSGLHQVPSQSPFpQHPFVPGGPP 473
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387 2380 SQDPFSSPQVTMQENFVRPQTPKHSGLSDDGfAQPQSNPASQTPVH 2425
Cdd:pfam03154  474 PITPPSGPPTSTSSAMPGIQPPSSASVSSSG-PVPAAVSCPLPPVQ 518
HMG smart00398
high mobility group;
1682-1735 3.67e-06

high mobility group;


Pssm-ID: 197700 [Multi-domain]  Cd Length: 70  Bit Score: 47.31  E-value: 3.67e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387  1682 APVLYTNMNFPNLKEEFPDWST--RVKQIAKLWRKASSQERSPYVQKARDNRAALR 1735
Cdd:smart00398    8 AFMLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
4885-4974 3.83e-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: 51.64  E-value: 3.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4885 VIEYIGTIIRNEVANRKEKmyesqnRGVYMFRID-------------------------------SEHVIDATITGGPAR 4933
Cdd:cd10545    112 ICEYVGELLDTSEADTRSG------NDDYLFDIDnrqtnrgwdggqrldvgmsdgerssaedeesSEFTIDAGSFGNVAR 185
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387 4934 YINHSCAPNCVAEVVTFEKGH----KIIISSNRKIQRGEELCYDY 4974
Cdd:cd10545    186 FINHSCSPNLFVQCVLYDHNDlrlpRVMLFAADNIPPLQELTYDY 230
PHD2_KMT2A_like cd15507
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
991-1041 4.35e-06

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: 46.69  E-value: 4.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  991 CTVCEACGQASDPgrLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCVSC 1041
Cdd:cd15507      2 CHVCGRKGQAQKQ--LLECEKCQRGYHVDCLGPSYPTKPTRKKKTWICSKC 50
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
4857-4996 4.74e-06

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


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 49.20  E-value: 4.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4857 WKTNVYLARSRiQGLGLYAARDIEKYTMVIEYIGTIIRNEvanrKEKMYESQNRG-----VYMFRIDSEHVIDatitgGP 4931
Cdd:cd10524      7 CPCNRYSLENH-YGAKIIATKPIKKGEKIHELCGCIAELS----EEEEALLRPGGndfsvMYSSRKKCSQLWL-----GP 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1658251387 4932 ARYINHSCAPNCvaEVVTFEKGhKIIISSNRKIQRGEEL-CY---DYkFDLEDdqhkipCHCGAVNCRK 4996
Cdd:cd10524     77 AAFINHDCRPNC--KFVPTGKS-TACVKVLRDIEPGEEItVYygdNY-FGENN------EECECETCER 135
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
1864-2235 5.07e-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: 52.65  E-value: 5.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1864 TPQPTNGSTsPVQHMVPKDSLAcSQLPGTPTSGSLDDVflRPQPPPPTGTRLTEACSQGQASQPQSPQMFSTGTASSSSR 1943
Cdd:pfam17823   91 TPHGTDLSE-PATREGAADGAA-SRALAAAASSSPSSA--AQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAAS 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1944 psspwdpyAKMVGTPRPPPIGSSTPRRNSTESCSAPrlpseqqergrPSSGhesfGSPTSASVDPYakppdtpRPAVTAd 2023
Cdd:pfam17823  167 --------APHAASPAPRTAASSTTAASSTTAASSA-----------PTTA----ASSAPATLTPA-------RGISTA- 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2024 pfVKPMGPPKAGIVLESQGRHMPASVIGDAFARPSHRAEAYQRMSHNKMV--------LSDPYSKpllTPIPgSNESGSV 2095
Cdd:pfam17823  216 --ATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVasaagtinMGDPHAR---RLSP-AKHMPSD 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2096 PLFKAPMPPPHPQdlynstpsigrrnsvdsferptrLSDTFSQNSQNDPYAH--PPLTPCTSMNDNFSNSPKMMHHPQSN 2173
Cdd:pfam17823  290 TMARNPAAPMGAQ-----------------------AQGPIIQVSTDQPVHNtaGEPTPSPSNTTLEPNTPKSVASTNLA 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2174 AF-----------CQPMPmVRHPSRDAFAQASSTSrsdfTQKSPDPYTQ---PPGTPRPSDPYAQ--PPG------TPRP 2231
Cdd:pfam17823  347 VVtttkaqakepsASPVP-VLHTSMIPEVEATSPT----TQPSPLLPTQgaaGPGILLAPEQVATeaTAGtasagpTPRS 421

                   ....
gi 1658251387 2232 AYDP 2235
Cdd:pfam17823  422 SGDP 425
PHD2_PHF12_Rco1 cd15534
PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...
993-1035 5.13e-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: 5.13e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1658251387  993 VCEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVP-KGSWKC 1035
Cdd:cd15534      1 VCFKCNRSCRVAPLIQCDYCPLLFHLDCLDPPLTHPPaTGRWMC 44
PHD_PHF21A cd15523
PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...
390-435 5.32e-06

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: 46.23  E-value: 5.32e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15523      1 FCSVCRKSGE---LLMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43
PHD1_BPTF cd15559
PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...
994-1038 5.73e-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: 45.87  E-value: 5.73e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDpgrLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15559      2 CRVCHKLGD---LLCCETCSAVYHLECVDPPLEEVPEEDWQCEVC 43
PHD_Phf1p_Phf2p_like cd15502
PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 ...
991-1038 5.86e-06

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: 46.28  E-value: 5.86e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  991 CTVCEaCGQASDPGRLLLCDDCDISYHTYCLDPPLQT----VPKGSWKCKWC 1038
Cdd:cd15502      2 CIVCQ-RGHSPKSNRIVFCDGCNTPYHQLCHDPSIDDevveDPDAEWFCKKC 52
ePHD_JMJD2B cd15714
Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...
4488-4592 5.98e-06

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: 48.01  E-value: 5.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGL---TDgparllnldlDLWVHLNCALWSTEVYETQA--GALINVELALRRGLSIRCVYCQRT-----GAT 4557
Cdd:cd15714      1 CCLCNLRGGALqmtTD----------ERWVHVICAIAVPEARFLNVieRHPVDVSAIPEQRWKLKCVYCRKRmkkvsGAC 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1658251387 4558 SGCHRLRCTNVYHFTCALKAQCTFFKDK-----TMLCHAH 4592
Cdd:cd15714     71 IQCSYDHCSTSFHVTCAHAAGVVMEPDDwpyvvSITCFKH 110
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1855-2348 6.55e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.78  E-value: 6.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1855 PNSGNQSPMTPQPTNGSTSPVQHMVPKDSLACSQLPGTPTSG---------SLDDVFLRPQPPPPTGTRLTEACSQGQAS 1925
Cdd:PRK10263   377 PEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQpyyapapeqPAQQPYYAPAPEQPVAGNAWQAEEQQSTF 456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1926 QPQSPQMFSTGTASSSSRpsspwDPYAKMVGTPRPPPIGSSTPRRNSTESCSAPRLPSEQQE--RGRPSSGHESFGSPTS 2003
Cdd:PRK10263   457 APQSTYQTEQTYQQPAAQ-----EPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEekRAREREQLAAWYQPIP 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2004 ASV-DPYAKPPDTPRPAVTADPFVKP---MGPPKAGIVLESQGRHMPASVIGDAFARPSHRAEAYQRmshnKMVLSDPYS 2079
Cdd:PRK10263   532 EPVkEPEPIKSSLKAPSVAAVPPVEAaaaVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQV----KEGIGPQLP 607
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2080 KPLLTPIPGSNESGSvplFKAPMPPphpQDLYNSTPSIGRRNSVDSFERPT----------RLSDTFSQNSQN---DPYA 2146
Cdd:PRK10263   608 RPKRIRVPTRRELAS---YGIKLPS---QRAAEEKAREAQRNQYDSGDQYNddeidamqqdELARQFAQTQQQrygEQYQ 681
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2147 HPplTPCTSMNDNFSNSPKMMHH---PQSNAFCQPMPMVRHP-SRDAFAQASSTSRSDFTQKSP--DPYTQP---PGTPR 2217
Cdd:PRK10263   682 HD--VPVNAEDADAAAEAELARQfaqTQQQRYSGEQPAGANPfSLDDFEFSPMKALLDDGPHEPlfTPIVEPvqqPQQPV 759
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2218 PSDPYAQPPGTPRPAYDPYAQP--PGTPRPFDPYSKPPGTPRPASDSFSNsasrpggvdQYSPQQPSNRRSSPSHAMEPY 2295
Cdd:PRK10263   760 APQQQYQQPQQPVAPQPQYQQPqqPVAPQPQYQQPQQPVAPQPQYQQPQQ---------PVAPQPQYQQPQQPVAPQPQY 830
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 2296 PQPPGTPCPGTGERFSKsPVSQRNADSY-FQQPETPrLVKNDTYAQQPNIPKPV 2348
Cdd:PRK10263   831 QQPQQPVAPQPQDTLLH-PLLMRNGDSRpLHKPTTP-LPSLDLLTPPPSEVEPV 882
PHD_Phf1p_Phf2p_like cd15502
PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 ...
388-435 6.66e-06

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: 46.28  E-value: 6.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  388 CKVCQTCKNPGEDsKMLVCDTCDKGYHTFCLQPVMD----SIPTNGWRCKNC 435
Cdd:cd15502      2 CIVCQRGHSPKSN-RIVFCDGCNTPYHQLCHDPSIDdevvEDPDAEWFCKKC 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2113-2435 7.37e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.85  E-value: 7.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2113 STPSIGRRNSVDSFERPTRLSDTFSQNSQNDPYAHPPL-TPCTSMNDNFSNSPKMMHHPQSNAFCQPMPMVRHPS--RDA 2189
Cdd:pfam03154  111 NSPSEGEGESSDGRSVNDEGSSDPKDIDQDNRSTSPSIpSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSppPPG 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2190 FAQASSTSRSDFTQKSPdPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFsnSASR 2269
Cdd:pfam03154  191 TTQAATAGPTPSAPSVP-PQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP--QPLP 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2270 PGGVDQYSPQQPSNRRSSPSHAMEPY----------------PQPPGTPCPGTGERFSKSPVSQrnadSYFQQPETPRlv 2333
Cdd:pfam03154  268 QPSLHGQMPPMPHSLQTGPSHMQHPVppqpfpltpqssqsqvPPGPSPAAPGQSQQRIHTPPSQ----SQLQSQQPPR-- 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2334 kndtyaQQPNIPKPVLSDPYSQPPGTPRPGV-------------GPEVFNRPVARTGPVSQDPFSS------------PQ 2388
Cdd:pfam03154  342 ------EQPLPPAPLSMPHIKPPPTTPIPQLpnpqshkhpphlsGPSPFQMNSNLPPPPALKPLSSlsthhppsahppPL 415
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 2389 VTMQENFVRPQTP-------KHSGLSDDGFAQPQSNPASQTPVHDPYAQAPMTP 2435
Cdd:pfam03154  416 QLMPQSQQLPPPPaqppvltQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVP 469
PHD3_PHF14 cd15563
PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
390-435 9.41e-06

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: 45.46  E-value: 9.41e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTN---GWRCKNC 435
Cdd:cd15563      1 ECCVCKQTGDNSQLVRCDECKLCYHFGCLDPPLKKSPKQrgyGWVCEEC 49
PHD1_KMT2C_like cd15509
PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
944-991 9.45e-06

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: 45.76  E-value: 9.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  944 CVVCGSFGQGAEgrLLACSQCGQCYHPYCVN--IKITRVVLSkGWRCLEC 991
Cdd:cd15509      2 CAVCDSPGDLSD--LLFCTSCGQHYHGSCLDpaVRPTPLVRA-GWQCPEC 48
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1860-2262 1.17e-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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.08  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1860 QSPMTPQPTNGSTSPVQHMVPKDSLACSQLPgTPTSGSLDdvflrPQPPPPTGTrlteacSQGQASQPQSPQMFSTGTAS 1939
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGP-TPSAPSVP-----PQGSPATSQ------PPNQTQSTAAPHTLIQQTPT 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1940 SSSRPSSPwdPYAKMVGTPRPPPigsstPRRNSTESCSAPRLPSEQQERGRPSSGHESFgSPTSASVDPYAKPPDTPRPA 2019
Cdd:pfam03154  237 LHPQRLPS--PHPPLQPMTQPPP-----PSQVSPQPLPQPSLHGQMPPMPHSLQTGPSH-MQHPVPPQPFPLTPQSSQSQ 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2020 VtadpfvkPMGPPKAGIVLESQGRHMPasvigdafarPSHRAEAYQRMSHNKMVLSDPYSKPLLTPIPgsnesgSVPLFK 2099
Cdd:pfam03154  309 V-------PPGPSPAAPGQSQQRIHTP----------PSQSQLQSQQPPREQPLPPAPLSMPHIKPPP------TTPIPQ 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2100 APMPPPHPQDLYNSTPSIGRRNSvdSFERPTRLSDTFSQNSQNDPYAHPP---LTPCTSMNDNFSNSPKMMHHPQSnafc 2176
Cdd:pfam03154  366 LPNPQSHKHPPHLSGPSPFQMNS--NLPPPPALKPLSSLSTHHPPSAHPPplqLMPQSQQLPPPPAQPPVLTQSQS---- 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2177 QPMPMVRHPSRDAFAQASSTS---RSDFTQKSPDPYTQPPGTP---RPSDPYAQPPGTPRPAYD-----------PYAQ- 2238
Cdd:pfam03154  440 LPPPAASHPPTSGLHQVPSQSpfpQHPFVPGGPPPITPPSGPPtstSSAMPGIQPPSSASVSSSgpvpaavscplPPVQi 519
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1658251387 2239 -------------PPGTPRPFDPYSKPPGTPRPASDS 2262
Cdd:pfam03154  520 keealdeaeepesPPPPPRSPSPEPTVVNTPSHASQS 556
PHD1_MTF2_PHF19_like cd15499
PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...
388-435 1.25e-05

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: 45.57  E-value: 1.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  388 CKVCQTcKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNG---WRCKNC 435
Cdd:cd15499      2 CSICGG-AEARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGdekWFCSRC 51
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
2001-2316 1.29e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 51.60  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2001 PTSASVDPYAKPP--DTPRPAVTADPFVKPMGPPKAGIVLESQGRHMPASVIGDAFARPSHRAEAYQRMSHNKMVLSDPY 2078
Cdd:COG5180    116 PELAAGALPAPAAaaALPKAKVTREATSASAGVALAAALLQRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRDALKDS 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2079 SKPLLTPIPGSNESGSVPLFKAPMPPPHPQDLYNSTP---------SIGRRNSVDSFERPTRLSDTFSQNSQ---NDPYA 2146
Cdd:COG5180    196 PEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAASSPkvdppstseARSRPATVDAQPEMRPPADAKERRRAaigDTPAA 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2147 HPPLTPCTSmndnfsNSPKmmhhPQSNAFCQPMPMVRHPSRDAFAQASSTSrsdftqKSPDPYTQPPGTPRPSDPYAQPP 2226
Cdd:COG5180    276 EPPGLPVLE------AGSE----PQSDAPEAETARPIDVKGVASAPPATRP------VRPPGGARDPGTPRPGQPTERPA 339
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2227 GTPRPAyDPYAQPPGTPRPFDP----YSKPPGTPRPASDSFSNSASRPGGVdqySPQQPSNRRSSPSHAMEPYPQPPGTP 2302
Cdd:COG5180    340 GVPEAA-SDAGQPPSAYPPAEEavpgKPLEQGAPRPGSSGGDGAPFQPPNG---APQPGLGRRGAPGPPMGAGDLVQAAL 415
                          330
                   ....*....|....
gi 1658251387 2303 CPGTGERFSKSPVS 2316
Cdd:COG5180    416 DGGGRETASLGGAA 429
PHA03379 PHA03379
EBNA-3A; Provisional
2165-2436 1.31e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 51.98  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2165 KMMHHPQSNAFCQPMPMVRHPsRDAFAQASSTSRSDFTQKSPDPYTQPPGTPRPSD--------PYAQPPGTPRPAYDPY 2236
Cdd:PHA03379   403 EALEKASEPTYGTPRPPVEKP-RPEVPQSLETATSHGSAQVPEPPPVHDLEPGPLHdqhsmapcPVAQLPPGPLQDLEPG 481
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2237 AQPPGTPRpfDPYSKPPGTPRPASdsfsnSASRPGgvdQYSPQQpsnrrsSPSHAMEPY-PQP-PGTPCPGTGERFSKsP 2314
Cdd:PHA03379   482 DQLPGVVQ--DGRPACAPVPAPAG-----PIVRPW---EASLSQ------VPGVAFAPVmPQPmPVEPVPVPTVALER-P 544
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2315 VSQRNADSYFQQPETPRLVK--NDTYAQQPNIPKPVlsDPYSQPPGTPRPGVG-PEVFnrpvARTGPVSQDPFSSPQVTM 2391
Cdd:PHA03379   545 VCPAPPLIAMQGPGETSGIVrvRERWRPAPWTPNPP--RSPSQMSVRDRLARLrAEAQ----PYQASVEVQPPQLTQVSP 618
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 2392 QENFVRPQTPKHSGLSDDGFAQPQSN------PASQTPVHDPYAQAPMTPR 2436
Cdd:PHA03379   619 QQPMEYPLEPEQQMFPGSPFSQVADVmraggvPAMQPQYFDLPLQQPISQG 669
PHD_PHF21B cd15524
PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) ...
994-1038 1.31e-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: 1.31e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQASDpgrLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15524      2 CAACKRGGN---LQPCGTCPRAYHLDCLDPPLKTAPKGVWVCPKC 43
PHD_UHRF2 cd15617
PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...
391-435 1.49e-05

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


Pssm-ID: 277089  Cd Length: 47  Bit Score: 44.95  E-value: 1.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTN-GWRCKNC 435
Cdd:cd15617      2 CYVCGGKQDAHMQLLCDECNMAYHIYCLNPPLDKIPEDeDWYCPSC 47
PHD3_KMT2A_like cd15508
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
1071-1108 1.51e-05

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: 45.13  E-value: 1.51e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1658251387 1071 CPIC--CHDYRQ-DELIVQCRQCDRWMHACCQNLnSDEEVE 1108
Cdd:cd15508      2 CPLCekCYDDDDyDSKMMQCSQCDHWVHAKCEGL-SDEMYE 41
PHD2_PHF14 cd15562
PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
390-435 1.87e-05

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: 44.70  E-value: 1.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIP----TNGWRCKNC 435
Cdd:cd15562      1 SCGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTRMPkktkNSGWQCSEC 50
PHD1_MTF2_PHF19_like cd15499
PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...
993-1041 2.46e-05

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: 44.41  E-value: 2.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  993 VCEACG--QASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWCVSC 1041
Cdd:cd15499      1 TCSICGgaEARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGDEKWFCSRC 51
PHA03377 PHA03377
EBNA-3C; Provisional
1965-2479 2.47e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 50.82  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1965 SSTPRR-NSTESCSAPRLPSEQQERGRPSS-GHESFGSPTSASVDPYAKPPDTPRPA--VTADPFV-------------- 2026
Cdd:PHA03377   447 QSTPERpGPSDQPSVPVEPAHLTPVEHTTViLHQPPQSPPTVAIKPAPPPSRRRRGAcvVYDDDIIevidvetteeeesv 526
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2027 ----KPMGPPKAGIVL--ESQGRHMPASVIGDAFARPSHRAEAYQRMSHNKMVLSDPYSKPLLTPIPGSNESGSVPLFK- 2099
Cdd:PHA03377   527 tqpaKPHRKVQDGFQRsgRRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDg 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2100 APMPPPHPQDLYNSTPSIGRRNSVDSFERPTRLSDTFSqnsqndpyahpPLTPCTSMNDNFSNSPKMMHHPQSNAFCQPM 2179
Cdd:PHA03377   607 PPASGPHEKQPPSSAPRDMAPSVVRMFLRERLLEQSTG-----------PKPKSFWEMRAGRDGSGIQQEPSSRRQPATQ 675
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2180 PMVRHPSR-----------DAFAQASSTSR-SDFTQKSPDPYTQPPGTPRPSD-------PYAQPPGTPRPAYDPYAQPP 2240
Cdd:PHA03377   676 STPPRPSWlpsvfvlpsvdAGRAQPSEESHlSSMSPTQPISHEEQPRYEDPDDpldlslhPDQAPPPSHQAPYSGHEEPQ 755
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2241 GTPRPFDPYSKPPGTPRP------ASDSFSNSASRPGGVDQYS--PQQPSNRRSSPSHAMEPYPQPPGTP----CPGTGE 2308
Cdd:PHA03377   756 AQQAPYPGYWEPRPPQAPylgyqePQAQGVQVSSYPGYAGPWGlrAQHPRYRHSWAYWSQYPGHGHPQGPwaprPPHLPP 835
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2309 RFSKSPVSQRNADSYFQ--QPET--PRLvkndTYAQQPNIPKPVLSDPYSQPPGTPRPgvgPEVFNRPVARTGPVSQDPF 2384
Cdd:PHA03377   836 QWDGSAGHGQDQVSQFPhlQSETgpPRL----QLSQVPQLPYSQTLVSSSAPSWSSPQ---PRAPIRPIPTRFPPPPMPL 908
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2385 SSPQVT--MQENFVRPQTPKHSGLSDDGFAQPQSNpasqtpvhdpyAQAPMTPRPQLGD----RLAREVKDQVEVGHEGS 2458
Cdd:PHA03377   909 QDSMAVgcDSSGTACPSMPFASDYSQGAFTPLDIN-----------AQTPKRPRVEESShgpaRCSQATTEAQEILSDNS 977
                          570       580
                   ....*....|....*....|.
gi 1658251387 2459 SHGVGQFSNLQQSTSNSTESQ 2479
Cdd:PHA03377   978 EISVFPKDAKQTDYDASTESE 998
PHD3_PHF14 cd15563
PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
343-388 2.51e-05

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: 44.31  E-value: 2.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  343 NCAVCDSPGDLLDQLFCTTCGQHYHGTCLDigvTPLKRA------GWQCPEC 388
Cdd:cd15563      1 ECCVCKQTGDNSQLVRCDECKLCYHFGCLD---PPLKKSpkqrgyGWVCEEC 49
PHD_PRHA_like cd15504
PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...
987-1038 2.60e-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: 44.35  E-value: 2.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387  987 RCLECTVceacGQASDPGRLLLCD-DCDISYHTYCLDPPLQT--VPKG--SWKCKWC 1038
Cdd:cd15504      1 FCAKCQS----GEASPDNDILLCDgGCNRAYHQKCLEPPLLTedIPPEdeGWLCPLC 53
PHD3_KMT2A cd15592
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
1070-1120 2.79e-05

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: 44.59  E-value: 2.79e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387 1070 VCPICCHDYRQDEL---IVQCRQCDRWMHACCQNLNSD--EEVENVADD-GFECAMC 1120
Cdd:cd15592      1 FCPLCDKCYDDDDYeskMMQCGKCDRWVHSKCENLSDEmyEILSNLPESvAYTCINC 57
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
4515-4578 3.38e-05

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: 46.11  E-value: 3.38e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4515 HLNCALWSTEVYETQAG-------ALINVELALRRGLSIRCVYCQRTGATSGCHRLRCTNVYHFTCAL--KAQ 4578
Cdd:cd15710     26 HHKCMLFSSALVSSHSDsenlggfSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCALhdKAQ 98
PHD1_Snt2p_like cd15497
PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...
994-1038 3.74e-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: 43.84  E-value: 3.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVP-KG-SWKCKWC 1038
Cdd:cd15497      2 CKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPnRGfVWSCAPC 48
PTZ00395 PTZ00395
Sec24-related protein; Provisional
2254-2480 3.94e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 50.46  E-value: 3.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2254 GTPRPAS-DSFSNSASRPGGVDQYSPQQPSNRrsspsHAMEPYPQPPGTPCPGTGERFSKSPVSQRNAdSYFQQPETPRL 2332
Cdd:PTZ00395   345 GSPNAASaGAPFNGLGNQADGGHINQVHPDAR-----GAWAGGPHSNASYNCAAYSNAAQSNAAQSNA-GFSNAGYSNPG 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2333 VKNDTYAQQPNIPKPVLSDPYSQPPGTPRPGVGPEVFNRPVARTgPVSQDPFS-SPQVTMQENFVRPQTP-KHSGLSDDG 2410
Cdd:PTZ00395   419 NSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNT-PYSNAPLSnAPPSSAKDHHSAYHAAyQHRAANQPA 497
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 2411 FAQPQSNPASQTPVH--------DPYAQAPMTPRPQLGDRlAREVKDQVEVGHEGSSHGVGQFSNLQQSTSNSTESQS 2480
Cdd:PTZ00395   498 ANLPTANQPAANNFHgaagnsvgNPFASRPFGSAPYGGNA-ATTADPNGIAKREDHPEGGTNRQKYEQSDEESVESSS 574
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
4513-4622 4.10e-05

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 49.98  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4513 WVHLNCALWSTEVYETQAGALINVELALRRGLS---IRCVYCQ-RTGATSGCHRLRCTNVYHFTCALKAqCTFFK----- 4583
Cdd:COG5141    268 WGHVICAMFNPELSFGHLLSKDPIDNIASVSSSrwkLGCLICKeFGGTCIQCSYFNCTRAYHVTCARRA-GYFDLniysh 346
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387 4584 -------DKTMLCHAHKPRgGGGQEHELRYFAvFRRVYVQR--DEVRQ 4622
Cdd:COG5141    347 ngisyciDHEPLCRKHYPL-GYGRMNGLRYFG-YEKLRYKNppTAIPR 392
PHD1_MOZ_d4 cd15526
PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 ...
957-991 4.32e-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: 43.88  E-value: 4.32e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1658251387  957 RLLACSQCGQCYHPYCVNI--KITRVVLSKGWRCLEC 991
Cdd:cd15526     20 ELISCADCGSSGHPSCLKFspGLTDAVKSYRWQCIEC 56
PHD1_Snt2p_like cd15497
PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...
391-435 4.97e-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: 43.45  E-value: 4.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  391 CQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNG--WRCKNC 435
Cdd:cd15497      2 CKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPNRGfvWSCAPC 48
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
1070-1120 5.66e-05

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: 43.46  E-value: 5.66e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 1070 VCPICCHDYRQDELIVQCRQCDRWMHACCQNLNSDEEVENvadDGFECAMC 1120
Cdd:cd15489      1 SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPN---GKWICPVC 48
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2183-2342 6.13e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 6.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2183 RHPSRDAFAQASSTSRSDFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPfDPYSKPPGTPRPASDS 2262
Cdd:PRK07764   637 AEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPA-QPAPAPAATPPAGQAD 715
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2263 FSNSASRPGGVDQYSPQQPSNRRSSPSHAMEPYPQPPGTPCPGTGERFSKSPVSQRNADSYFQQPETPRLVKNDTYAQQP 2342
Cdd:PRK07764   716 DPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDD 795
PHD2_PHF14 cd15562
PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
344-388 6.37e-05

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: 43.16  E-value: 6.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  344 CAVCDSPGD--LLDQlfCTTCGQHYHGTCLDIGVT--PLKRA--GWQCPEC 388
Cdd:cd15562      2 CGICKKSNDqhLLAL--CDTCKLYYHLGCLDPPLTrmPKKTKnsGWQCSEC 50
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2190-2424 7.12e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 49.10  E-value: 7.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2190 FAQASSTSRSDFTQkSPDPYT---------------QPPGTPRPSDPYAQPPGTPRPAydPYAQPPGTPRPFDPYSKPPG 2254
Cdd:PRK12323   332 FYQIANLGRSELAL-APDEYAgftmtllrmlafrpgQSGGGAGPATAAAAPVAQPAPA--AAAPAAAAPAPAAPPAAPAA 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2255 TPRPA----SDSFSNSASRPGGVDQYSPQQPSNRRSSPshAMEPYPQPPGTPCPGTgerfsKSPVSQRNADSYFQQPETP 2330
Cdd:PRK12323   409 APAAAaaarAVAAAPARRSPAPEALAAARQASARGPGG--APAPAPAPAAAPAAAA-----RPAAAGPRPVAAAAAAAPA 481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2331 RLVKNDTYAQQPNIPKP--------VLSDPYSQPPG--------TPRPGVGPEVFNRPVARTGPVsqdPFSSPQVTMQEN 2394
Cdd:PRK12323   482 RAAPAAAPAPADDDPPPweelppefASPAPAQPDAApagwvaesIPDPATADPDDAFETLAPAPA---AAPAPRAAAATE 558
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1658251387 2395 FVRPQTPKHSGLS--DDGFAQPQSNPASQTPV 2424
Cdd:PRK12323   559 PVVAPRPPRASASglPDMFDGDWPALAARLPV 590
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
1070-1123 8.03e-05

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: 43.25  E-value: 8.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 1070 VCPICcHDYRQDELIVQCRQCDRWMHACCqnLNSDEEVENVADDGFECAMCHVR 1123
Cdd:pfam00628    1 YCAVC-GKSDDGGELVQCDGCDDWFHLAC--LGPPLDPAEIPSGEWLCPECKPK 51
PHD1_KMT2C_like cd15509
PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
994-1038 8.53e-05

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: 43.07  E-value: 8.53e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  994 CEACGQASDPGRLLLCDDCDISYHTYCLDPPLQTVP--KGSWKCKWC 1038
Cdd:cd15509      2 CAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVRPTPlvRAGWQCPEC 48
HMG_box pfam00505
HMG (high mobility group) box;
1684-1735 9.06e-05

HMG (high mobility group) box;


Pssm-ID: 459837 [Multi-domain]  Cd Length: 68  Bit Score: 43.37  E-value: 9.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 1684 VLYTNMNFPNLKEEFPDWSTR--VKQIAKLWRKASSQERSPYVQKARDNRAALR 1735
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62
PHD_PRKCBP1 cd15538
PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...
955-991 1.12e-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: 42.31  E-value: 1.12e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1658251387  955 EGRLLACSQCGQCYHPYCVNIKITrvvLSKGWRCLEC 991
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 ...
4513-4576 1.16e-04

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277141  Cd Length: 112  Bit Score: 44.36  E-value: 1.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658251387 4513 WVHLNCALWSTEV-------YEtqagALINVELALRRGLSIRCVYCQ-RTGATSGCHRLRCTNVYHFTCALK 4576
Cdd:cd15671     20 WVHVSCALWIPEVsigcpekME----PITKISHIPMSRWALVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQ 87
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
390-435 1.20e-04

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: 42.33  E-value: 1.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15541      1 WCAVCQNGGE---LLCCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC 43
PHD_Int12 cd15501
PHD finger found in integrator complex subunit 12 (Int12) and similar proteins; Int12, also ...
944-991 1.21e-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: 42.72  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658251387  944 CVVCGSFGQGAEGRLLACSQCGQCYHPYCVNIKIT-------RVVlskgWRCLEC 991
Cdd:cd15501      2 CVVCKQMDVTSGNQLVECQECHNLYHQECHKPPVTdkdvndpRLV----WYCSRC 52
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
990-1037 1.52e-04

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 41.93  E-value: 1.52e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  990 ECTVCEacgqasDPGRLLLCD--DCDISYHTYCLDppLQTVPKGSWKCKW 1037
Cdd:cd15568      1 ECFRCG------DGGDLVLCDfkGCPKVYHLSCLG--LEKPPGGKWICPW 42
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2189-2307 1.54e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2189 AFAQASSTSRSDFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDsfsnSAS 2268
Cdd:PRK07764   389 GGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA----PSA 464
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1658251387 2269 RPGGVDQYSPQQPSNRRSSPSHAMEPYPQPPGTPCPGTG 2307
Cdd:PRK07764   465 QPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAP 503
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
4861-4980 1.54e-04

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).


Pssm-ID: 380938  Cd Length: 112  Bit Score: 44.17  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4861 VYLARSRIQGLGLYAARDIEKYTmVIEYIGTIIrneVANRKEKMYESQNRGVYMFRIDSEHVIDATITGGparYINHSCA 4940
Cdd:cd10540      2 LEVKPSTLKGRGVFATRPIKKGE-VIEEAPVIV---LPKEEYQHLCKTVLDHYVFSWGDGCLALALGYGS---MFNHSYT 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1658251387 4941 PNcvAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLED 4980
Cdd:cd10540     75 PN--AEYEIDFENQTIVFYALRDIEAGEELTINYGDDLWD 112
PHD_TIF1beta cd15623
PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also ...
994-1038 1.60e-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: 1.60e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQasdPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15623      2 CRVCQK---AGALVMCDQCEFCFHLDCHLPALQEVPGEDWKCLLC 43
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
4513-4592 1.90e-04

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: 43.86  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4513 WVHLNCALWSTEVY--ETQAGALI-NVELALRRGLSIRCVYC-QRTGATSGCHRLRCTNVYHFTCALKA----------- 4577
Cdd:cd15670     19 WAHVVCALWIPEVSfaNTVFLEPIdGIQNIPKARWKLTCYICkKRMGACIQCHKKNCYTAFHVTCAQQAglymkiepvkd 98
                           90
                   ....*....|....*...
gi 1658251387 4578 ---QCTFFKDKTMLCHAH 4592
Cdd:cd15670     99 pgnGTSDSVRKEAYCDKH 116
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
344-388 1.95e-04

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: 41.98  E-value: 1.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  344 CAVCDSPGDLLDQLFCTTCGQHYHGTCLDIGVTPLKRAGWQCPEC 388
Cdd:cd15527      2 CSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46
PHD3_KMT2B cd15593
PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
1071-1108 2.20e-04

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: 42.14  E-value: 2.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1658251387 1071 CPICCHDYRQDEL---IVQCRQCDRWMHACCQNLnSDEEVE 1108
Cdd:cd15593      2 CPICLKCYEDNDYeskMMQCAKCDHWVHAKCEGL-SDELYE 41
PHD_PHF21A cd15523
PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...
344-388 2.47e-04

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


Pssm-ID: 276998 [Multi-domain]  Cd Length: 43  Bit Score: 41.61  E-value: 2.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  344 CAVCDSPGDLLdqlFCTTCGQHYHGTCLDIGVTPLKRAGWQCPEC 388
Cdd:cd15523      2 CSVCRKSGELL---MCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43
PHD_PRHA_like cd15504
PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...
390-435 2.57e-04

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: 41.65  E-value: 2.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658251387  390 VCQTCKNP--GEDSKMLVCD-TCDKGYHTFCLQPVMDSI----PTNGWRCKNC 435
Cdd:cd15504      1 FCAKCQSGeaSPDNDILLCDgGCNRAYHQKCLEPPLLTEdippEDEGWLCPLC 53
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
4488-4584 2.61e-04

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: 43.92  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHE-EGDGLTDGPARLLNLDlDLWVHLNCALWST---EVYETQAGALINVELA-----LRRGLSIRCVYCQRTGATS 4558
Cdd:cd15711      1 CGFCHAgEEENETRGKLHIFNAK-KAAAHYKCMLFSSgtvQLTTTSRAEFGDFDIKtviqeIKRGKRMKCTLCSQLGATI 79
                           90       100
                   ....*....|....*....|....*.
gi 1658251387 4559 GCHRLRCTNVYHFTCALKAQCTFFKD 4584
Cdd:cd15711     80 GCEIKACVKTYHYHCGVQDKAKYIEN 105
HMG-box_BHMG1 cd21977
high mobility group (HMG)-box found in basic helix-loop-helix and HMG box domain-containing ...
1684-1738 2.70e-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: 41.92  E-value: 2.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 1684 VLYTNMNFPNLKEEFPDWSTRV--KQIAKLWRKASSQERSPYVQKARD-NRAALRINK 1738
Cdd:cd21977      9 IMFCRLNRKNYIDKHPGLASTEltKELGQLWRELSAEEKKPYCVRARElSQLHNRKVK 66
ePHD_JMJD2B cd15714
Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...
285-315 2.77e-04

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: 43.39  E-value: 2.77e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1658251387  285 CAYCKR-----LGASIKCCQEECSRSYHYPCAAAAG 315
Cdd:cd15714     56 CVYCRKrmkkvSGACIQCSYDHCSTSFHVTCAHAAG 91
PHD4_KMT2C cd15596
PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
344-388 2.96e-04

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: 41.54  E-value: 2.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  344 CAVCDSPGDLLDQ--LFCTTCGQHYHGTCLDIGVTP-LKRAGWQCPEC 388
Cdd:cd15596      9 CVVCGSFGQGAEGrlLACSQCGQCYHPYCVSIKITKvVLSKGWRCLEC 56
PHD5_NSD3 cd15661
PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
997-1037 3.40e-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: 41.11  E-value: 3.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1658251387  997 CGQASDPGRLLLCD--DCDISYHTYCLDppLQTVPKGSWKCKW 1037
Cdd:cd15661      2 CFQCGDGGELVMCDkkDCPKAYHLLCLN--LTQPPYGKWECPW 42
PHD1_MTF2 cd15578
PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also ...
388-435 3.55e-04

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: 41.23  E-value: 3.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387  388 CKVCQTcKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSI---PTNGWRCKNC 435
Cdd:cd15578      2 CTVCQD-GSSESPNEIVLCDKCGQGYHQLCHNPKIDSSvldPDVPWLCRQC 51
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
4873-4994 3.58e-04

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: 44.23  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4873 LYAARDIEKYTMVIEYIGTII---RNEVANRKEK------MYESQNRGVYMfridsehVIDATITGGPARYINHSCAPNC 4943
Cdd:cd19181     21 LRAARDLALDTLIIEYRGKVMlrqQFEVNGHFFKrpypfvLFYSKFNGVEM-------CVDARTFGNDARFIRRSCTPNA 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658251387 4944 VAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFDLEDDQHKIPCHC--GAVNC 4994
Cdd:cd19181     94 EVRHMIADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCAChkGNRNC 146
ePHD_ATX1_2_like cd15662
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...
251-330 3.66e-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: 43.23  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  251 AHQRCAVWSRGVCRGEGTSLLNVD--KAIDSGSTE-SCAYCK-RLGASIKCCQEECSRSYHYPCAAAAGTFQDFR----- 321
Cdd:cd15662     20 AHLACAIWIPETCLLDVKTMEPVDgiNAISKERWElSCTICKqRYGACIQCSNNSCRVAYHPLCARAAGLCMEVAdegge 99
                           90
                   ....*....|....*.
gi 1658251387  322 -------KLTLLCPKH 330
Cdd:cd15662    100 dpgdqglRLLSYCPRH 115
dnaA PRK14086
chromosomal replication initiator protein DnaA;
2170-2363 3.69e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 46.74  E-value: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2170 PQSNAFCQPM---PMVRHPSRDAFAqASSTSRSDFTQKSPDPYTQPPgTPRPSDPYAQPPGTP----RPAYD-PYAQPPG 2241
Cdd:PRK14086    95 PAPPPPHARRtsePELPRPGRRPYE-GYGGPRADDRPPGLPRQDQLP-TARPAYPAYQQRPEPgawpRAADDyGWQQQRL 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2242 TPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRRSS--PSHAMEPYPQPPgtpcPGTGERFSKSPVSqrn 2319
Cdd:PRK14086   173 GFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWdrPRRDRTDRPEPP----PGAGHVHRGGPGP--- 245
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1658251387 2320 adsyfqqPETPRlvkndtyAQQPNIPKPVLSDPYSQPPGTPRPG 2363
Cdd:PRK14086   246 -------PERDD-------APVVPIRPSAPGPLAAQPAPAPGPG 275
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
251-330 3.85e-04

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277141  Cd Length: 112  Bit Score: 43.20  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  251 AHQRCAVWSRGVCRGEGTSL---LNVDKAIDSGSTESCAYCK-RLGASIKCCQEECSRSYHYPCAAAAG--------TFQ 318
Cdd:cd15671     21 VHVSCALWIPEVSIGCPEKMepiTKISHIPMSRWALVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQHGlemktileDED 100
                           90
                   ....*....|..
gi 1658251387  319 DFRKLTLLCPKH 330
Cdd:cd15671    101 DEVKFKSYCPKH 112
PTZ00395 PTZ00395
Sec24-related protein; Provisional
2170-2287 3.87e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 46.99  E-value: 3.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2170 PQSNAfcqpmpmvrHPSRDAFAQA--SSTSRSDfTQKSPDPYTQPPGT-------PRPSDPYAQPPGTPRPAYDP-YAQP 2239
Cdd:PTZ00395   383 PHSNA---------SYNCAAYSNAaqSNAAQSN-AGFSNAGYSNPGNSnpgynnaPNSNTPYNNPPNSNTPYSNPpNSNP 452
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1658251387 2240 PGTPRPFD--PYSKPPGTPRPASD-----SFSNSASRPGGVDQYSPQQPSNRRSS 2287
Cdd:PTZ00395   453 PYSNLPYSntPYSNAPLSNAPPSSakdhhSAYHAAYQHRAANQPAANLPTANQPA 507
PostSET smart00508
Cysteine-rich motif following a subset of SET domains;
4983-4999 3.96e-04

Cysteine-rich motif following a subset of SET domains;


Pssm-ID: 214703  Cd Length: 17  Bit Score: 40.47  E-value: 3.96e-04
                            10
                    ....*....|....*..
gi 1658251387  4983 HKIPCHCGAVNCRKWMN 4999
Cdd:smart00508    1 KKQPCLCGAPNCRGFLG 17
PHD_TIF1delta cd15625
PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta); TIF1delta, also ...
391-436 4.25e-04

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: 41.10  E-value: 4.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  391 CQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNCR 436
Cdd:cd15625      5 CAVCLNGGE---LLCCDRCPKVFHLSCHVPALLSFPVGEWVCTLCR 47
PHD2_KMT2C_like cd15510
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...
944-991 4.72e-04

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: 40.88  E-value: 4.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  944 CVVCGSfgQGAEGRLLACSQCGQCYHPYCVNIKITRVVlSKGWRCLEC 991
Cdd:cd15510      2 CQACRQ--PGDDTKMLVCETCDKGYHTSCLRPVMSSIP-KYGWKCKNC 46
PHD_BRPF_JADE_like cd15492
PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; ...
993-1038 4.72e-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: 40.68  E-value: 4.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  993 VCEACGQAS--DPGRLLLCDDCDISYHTYCLDppLQTVPKGSWKCKWC 1038
Cdd:cd15492      1 VCDVCLDGEseDDNEIVFCDGCNVAVHQSCYG--IPLIPEGDWFCRKC 46
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
3256-3348 5.89e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.60  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3256 QKKQYEEWLQHTQ-QLLKMQQKFLEEQIGAHR---KSKKALSAKQRTAKKAgREFpEEDAEQLKHVTEQQSVVQKQLE-Q 3330
Cdd:pfam20492    7 EKQELEERLKQYEeETKKAQEELEESEETAEEleeERRQAEEEAERLEQKR-QEA-EEEKERLEESAEMEAEEKEQLEaE 84
                           90
                   ....*....|....*...
gi 1658251387 3331 IRKQQKEHAELIEEYRVK 3348
Cdd:pfam20492   85 LAEAQEEIARLEEEVERK 102
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
2170-2411 5.99e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.38  E-value: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2170 PQSNAFCQPMPMVRHPSRDAFAQASSTSRSDFTQKSPDPYTQP---PGTPRPSDPYAQPPGTPRPAydpyAQPPGTPRPf 2246
Cdd:PRK07003   412 PKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANaraSADSRCDERDAQPPADSGSA----SAPASDAPP- 486
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2247 dpysKPPGTPRPASDSFSNSASRPggVDQYSPQQPSNRRSSPSHAMEPYPQ-PPGTPCPGTGERFSKSPVSQ----RNA- 2320
Cdd:PRK07003   487 ----DAAFEPAPRAAAPSAATPAA--VPDARAPAAASREDAPAAAAPPAPEaRPPTPAAAAPAARAGGAAAAldvlRNAg 560
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2321 -----DSYFQQPETPRlvkndTYAQQPNIPKPVLSDPYSQPPgTPR-PGVGPEVFNRPVARTGPVSQDPFSSP--QVTMQ 2392
Cdd:PRK07003   561 mrvssDRGARAAAAAK-----PAAAPAAAPKPAAPRVAVQVP-TPRaRAATGDAPPNGAARAEQAAESRGAPPpwEDIPP 634
                          250
                   ....*....|....*....
gi 1658251387 2393 ENFVRPQTPKHSGLSDDGF 2411
Cdd:PRK07003   635 DDYVPLSADEGFGGPDDGF 653
PHD1_PHF10 cd15528
PHD finger 1 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
943-991 6.06e-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: 40.86  E-value: 6.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1658251387  943 MCVVC---GSFGQGAEGRLLACSQCGQCYHPYCVNI--KITRVVLSKGWRCLEC 991
Cdd:cd15528      1 VCGICekgGKSNKGEPEELIHCSQCGNSGHPSCLEMsdEMVAVIKTYPWQCMEC 54
ePHD_JMJD2 cd15675
Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
4488-4581 6.37e-04

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: 42.35  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGL---TDGparllnldldLWVHLNCALWSTEVY--ETQAGALINVELALRRGLSIRCVYCQR-------TG 4555
Cdd:cd15675      1 CCLCCLRGGALkptTDG----------RWAHVVCAIAIPEVRfsNVPERGPIDISKIPPARLKLKCIYCSKitksmshMG 70
                           90       100
                   ....*....|....*....|....*.
gi 1658251387 4556 ATSGCHRLRCTNVYHFTCALKAQCTF 4581
Cdd:cd15675     71 ACIQCSTGKCTTSFHVTCAHAAGVQM 96
PHD1_KMT2A_like cd15506
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
943-991 6.98e-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: 40.42  E-value: 6.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  943 MCVVCGSFGQGaegRLLACSQCGQCYHPYCVNIKITRVVLSKG-WRCLEC 991
Cdd:cd15506      1 LCFLCGSAGLN---ELLYCSVCCEPYHTFCLEEAERPLNINKDnWCCRRC 47
PHD1_MTF2 cd15578
PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also ...
991-1040 7.06e-04

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: 40.46  E-value: 7.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1658251387  991 CTVCEAcGQASDPGRLLLCDDCDISYHTYCLDPPLQTV---PKGSWKCKWCVS 1040
Cdd:cd15578      2 CTVCQD-GSSESPNEIVLCDKCGQGYHQLCHNPKIDSSvldPDVPWLCRQCVF 53
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
344-388 8.72e-04

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: 39.74  E-value: 8.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  344 CAVCDSPGDLLdqlFCTTCGQHYHGTCLDIGVTPLKRAGWQCPEC 388
Cdd:cd15539      2 CAVCGDGGELL---CCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43
PHA03247 PHA03247
large tegument protein UL36; Provisional
2171-2409 9.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 9.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2171 QSNAFCQPMPMVRHPSR-DAFAQASSTSRSDFTQKspdpytqPPGTPRPSDPYAQPPGTPRPAyDPYAQPP--------G 2241
Cdd:PHA03247   233 QDEPFVERRVVISHPLRgDIAAPAPPPVVGEGADR-------APETARGATGPPPPPEAAAPN-GAAAPPDgvwgaalaG 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2242 TPrPFDPYSKPPGTPRPASDSfSNSASRPGGVDQYSPQQPSNRRSSPshAMEPYPQPPGTPcPGTGERFSKSPVSQRNAD 2321
Cdd:PHA03247   305 AP-LALPAPPDPPPPAPAGDA-EEEDDEDGAMEVVSPLPRPRQHYPL--GFPKRRRPTWTP-PSSLEDLSAGRHHPKRAS 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2322 SYFQQPETPRLVKNDTYAQQPNIPKPVLSDPYSQPPGTPRPGVGPEVFNRPVARTGPVSQDPFS-SPQVTMQENFVRPQT 2400
Cdd:PHA03247   380 LPTRKRRSARHAATPFARGPGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDdGPAPPPERQPPAPAT 459

                   ....*....
gi 1658251387 2401 PKHSGLSDD 2409
Cdd:PHA03247   460 EPAPDDPDD 468
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1070-1120 9.22e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 39.89  E-value: 9.22e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  1070 VCPICcHDYRQDELIVQCRQCDRWMHA-CCQnlnsDEEVENVADDGFECAMC 1120
Cdd:smart00249    1 YCSVC-GKPDDGGELLQCDGCDRWYHQtCLG----PPLLEEEPDGKWYCPKC 47
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
994-1038 9.49e-04

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


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 39.54  E-value: 9.49e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQAsdpGRLLLCDDCDISYHTYCLDppLQTVPKGSWKCKWC 1038
Cdd:cd15567      2 CFICSEG---GSLICCESCPASFHPECLG--LEPPPEGKFYCEDC 41
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
390-435 1.01e-03

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53).


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 39.96  E-value: 1.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15522      1 ICPICKKPDDGSPMIGCDECDDWYHWECVGITDEPPEEDDWFCPKC 46
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
248-311 1.01e-03

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: 41.99  E-value: 1.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  248 QCCAHQRCAVWSRGVCRGEGTS--------LLNVDKAIDSGSTESCAYCKRLGASIKCCQEECSRSYHYPCA 311
Cdd:cd15711     24 KAAAHYKCMLFSSGTVQLTTTSraefgdfdIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCG 95
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
464-498 1.03e-03

second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410355  Cd Length: 55  Bit Score: 40.12  E-value: 1.03e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1658251387  464 DAGASCPLCGKPLGAEFLSDHLTCQSCKRYLHLEC 498
Cdd:cd20805      9 PSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSEC 43
PHD4_KMT2C_like cd15512
PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD domain 3 found in ...
398-435 1.13e-03

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: 39.75  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1658251387  398 GEDSKMLVCDTCDKGYHTFCLQ-PVMDSIPTNGWRCKNC 435
Cdd:cd15512     11 GAEGRLIACSQCGQCYHPYCVNvKVTKVILSKGWRCLDC 49
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
4513-4592 1.14e-03

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


Pssm-ID: 277173 [Multi-domain]  Cd Length: 118  Bit Score: 41.96  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4513 WVHLNCALWSTEVYETQAGALINVE-----LALRRGLSirCVYCQRTG--ATSGCHRLRCTNVYHFTCALKA-------- 4577
Cdd:cd15703     19 WAHVVCAIWIPEVCFANTVFLEPVEgvnniPPARWKLT--CYLCKQKGrgAAIQCHKVNCYTAFHVTCAQRAglfmkiep 96
                           90       100
                   ....*....|....*....|..
gi 1658251387 4578 -------QCTFFKDKTMLCHAH 4592
Cdd:cd15703     97 vretglnGTTFTVRKTAYCENH 118
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
3022-3424 1.14e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.38  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3022 VPTDHSGPGAQGSQLAGMPQN-SSLLMAPGHIQEVEMNPSVTIGhrmdPSPAVGTTMGNP---EFLQGPSVRPNY---GA 3094
Cdd:pfam09606   62 QPQGGQGNGGMGGGQQGMPDPiNALQNLAGQGTRPQMMGPMGPG----PGGPMGQQMGGPgtaSNLLASLGRPQMpmgGA 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3095 AGPQGEQIIPTGGQPMTHN---QQLMFSQGLNQQNRPLLLEEQPLLLQDLLDQERQEQQQQRQMQAMIRQRSNDSFFPni 3171
Cdd:pfam09606  138 GFPSQMSRVGRMQPGGQAGgmmQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADA-- 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3172 dfdaitdpimKAKMVALKGINKMMVQSSMGMPPMvmNRIQMGGQQGPEGVSAVPQQVIGQDGKLASQLPRRNPPNF--GP 3249
Cdd:pfam09606  216 ----------GAQMGQQAQANGGMNPQQMGGAPN--QVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGpgQP 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3250 GFVNDSQKKQYEEWLQHTQQLLKMQQKFLEEQIGAHRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQQSVVQKQLE 3329
Cdd:pfam09606  284 MGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAN 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3330 QIRKQQKEHAELIEEYRVKHLQcsMQQPPMVAGMQPQTVMLSGGPPINQPRMSPMMQM------QPYHN-----QPNAPR 3398
Cdd:pfam09606  364 PMQRGQPGMMSSPSPVPGQQVR--QVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMipspalIPSPSpqmsqQPAQQR 441
                          410       420
                   ....*....|....*....|....*...
gi 1658251387 3399 MsgIPGWHPGAP--RPIGPGVPAPMASQ 3424
Cdd:pfam09606  442 T--IGQDSPGGSlnTPGQSAVNSPLNPQ 467
PHD2_KMT2B cd15591
PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...
944-991 1.18e-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: 39.92  E-value: 1.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  944 CVVCGSFGQGAEgRLLACSQCGQCYHPYCV--NIKITRVVLSKGWRCLEC 991
Cdd:cd15591      2 CHVCGRKNKESK-PLLECERCRNCYHPACLgpNYPKPANRKKRPWICSAC 50
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
4935-4991 1.23e-03

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


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 43.83  E-value: 1.23e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1658251387 4935 INHSCAPNCvaeVVTFEkGHKIIISSNRKIQRGEEL--CYDYKF---DLED------DQHKIPCHCGA 4991
Cdd:cd10536    154 LNHSCDPNT---IRSFY-GNTIVVRATRPIKKGEEItiCYGPHFsrmKRSErqrllkEQYFFDCSCEA 217
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
4936-4974 1.27e-03

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: 43.51  E-value: 1.27e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1658251387 4936 NHSCAPNCVAevvTFEkGHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd19203    147 NHSCDPNCVI---VFN-GPHLLLRAIREIEVGEELTISY 181
PHD5_NSD2 cd15660
PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
997-1037 1.39e-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: 39.53  E-value: 1.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1658251387  997 CGQASDPGRLLLCDD--CDISYHTYCLDppLQTVPKGSWKCKW 1037
Cdd:cd15660      2 CFRCGDGGQLVLCDRksCTKAYHLSCLG--LTKRPFGKWECPW 42
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2180-2304 1.44e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2180 PMVRHPSRDAFA---QASSTSRSDFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFD----PYSKP 2252
Cdd:PRK12323   423 PARRSPAPEALAaarQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADddppPWEEL 502
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387 2253 PGTprPASDSFSNSASRPGGVDQYSPQQPSNRRSSPSHAmEPYPQPPGTPCP 2304
Cdd:PRK12323   503 PPE--FASPAPAQPDAAPAGWVAESIPDPATADPDDAFE-TLAPAPAAAPAP 551
PHD1_BPTF cd15559
PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...
391-435 1.58e-03

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: 39.32  E-value: 1.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15559      2 CRVCHKLGD---LLCCETCSAVYHLECVDPPLEEVPEEDWQCEVC 43
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
4873-4977 1.79e-03

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: 41.42  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4873 LYAARDIEKYTMVIEYIGTIIRNEV--AN-----RKEK--MYESQNRGVYMfridsehVIDATITGGPARYINHSCAPNC 4943
Cdd:cd19182     21 LKAAKDLPPDTLIIEYRGKFMLREQfeANgyffkRPYPfvLFYSKFHGLEM-------CVDARTFGNEARFIRRSCTPNA 93
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1658251387 4944 VAEVVTFEKGHKIIISSNRKIQRGEELCYDYKFD 4977
Cdd:cd19182     94 EVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFD 127
PHD2_PHF12_Rco1 cd15534
PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...
390-434 1.89e-03

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: 39.25  E-value: 1.89e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  390 VCQTCKNPGEDSKMLVCDTCDKGYHTFCLQPVMDSIPTNG-WRCKN 434
Cdd:cd15534      1 VCFKCNRSCRVAPLIQCDYCPLLFHLDCLDPPLTHPPATGrWMCPN 46
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
3342-3582 2.05e-03

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: 44.64  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3342 IEEyrvKHLQCSMQQPPMVAGMQPQTVMLSGGPPINQPRMSPMMQMQP-------YHN---------------------- 3392
Cdd:pfam09770   95 IEE---EQVRFNRQQPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPvrtgyekYKEpepipdlqvdaslwgvapkkaa 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3393 -QPNAPRMSGIPGWHPGAPRPIGP--GVPAPMASQAP---SANTVQPVQTANGGGAPHVKFDDNNPFSEGFQERERKERL 3466
Cdd:pfam09770  172 aPAPAPQPAAQPASLPAPSRKMMSleEVEAAMRAQAKkpaQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQ 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3467 REQQERQRVQLMQEVERQRALQQRMEMEQQGLLGPDGNQDTLSQMAfygtdLPRDFMQ-PQRPSAPQQMFPQQGVQPSfm 3545
Cdd:pfam09770  252 QPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPV-----QPTQILQnPNRLSAARVGYPQNPQPGV-- 324
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1658251387 3546 SSSPGtffmQTGERRPlignGSFSSEMGPSFRPKHLM 3582
Cdd:pfam09770  325 QPAPA----HQAHRQQ----GSFGRQAPIITHPQQLA 353
PHD1_NSD cd15564
PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
344-389 2.12e-03

PHD finger 1 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 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 first PHD finger.


Pssm-ID: 277039  Cd Length: 43  Bit Score: 38.86  E-value: 2.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1658251387  344 CAVCDSPGDLldqLFCT-TCGQHYHGTCLdiGVTPLKRAGWQCPECK 389
Cdd:cd15564      2 CQICEKPGKL---LTCEgPCCGHFHLDCL--GLSEQPDEPFKCDECT 43
PHD_TIF1beta cd15623
PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also ...
391-435 2.24e-03

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: 38.63  E-value: 2.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15623      2 CRVCQKAGA---LVMCDQCEFCFHLDCHLPALQEVPGEDWKCLLC 43
PHD_JADE1 cd15679
PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger ...
991-1038 2.25e-03

PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of the cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation, and as a transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277149 [Multi-domain]  Cd Length: 46  Bit Score: 38.90  E-value: 2.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  991 CTVCEAcGQASDPGRLLLCDDCDISYHTYCLDppLQTVPKGSWKCKWC 1038
Cdd:cd15679      2 CDVCQS-PDGEDGNEMVFCDKCNICVHQACYG--ILKVPEGSWLCRTC 46
PHA03378 PHA03378
EBNA-3B; Provisional
1974-2488 2.26e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1974 ESCSAPRLPSEQQERGRPSSGHES--FGSPTSASVDPYAKPPDTPRPAVTADPFVKPM-------GPPKAGI-------- 2036
Cdd:PHA03378   428 EEHRKKKAARTEQPRATPHSQAPTvvLHRPPTQPLEGPTGPLSVQAPLEPWQPLPHPQvtpvilhQPPAQGVqahgsmld 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2037 VLESQGRHMPASVIGDAFARPSHRAEAYQR----------MSHNKMVLSDPYSKPLLtPIPGSNesgsvPLFKAPMPPPH 2106
Cdd:PHA03378   508 LLEKDDEDMEQRVMATLLPPSPPQPRAGRRapcvytedldIESDEPASTEPVHDQLL-PAPGLG-----PLQIQPLTSPT 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2107 PQDLYNSTPS-IGRRNSV----DSFERPT---RLSDTFSQNSQNDPYAHPPLTPCTSMNDNFS--------NSPKMMHHP 2170
Cdd:PHA03378   582 TSQLASSAPSyAQTPWPVphpsQTPEPPTtqsHIPETSAPRQWPMPLRPIPMRPLRMQPITFNvlvfptphQPPQVEITP 661
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2171 QSNAFCQPMPMVRHPSRDAFAQASSTSRSDFTQKSP-------DPYTQPPGTPRPsdPYAQPPGTPRPAYDPYA--QPPG 2241
Cdd:PHA03378   662 YKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPpraptpmRPPAAPPGRAQR--PAAATGRARPPAAAPGRarPPAA 739
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2242 TPRPFDPYSKPPGTPRP---ASDSFSNSASRPGG-VDQYSPQQPSNRRSSPSHAMEPYPQPPGTPCPgtGERFSKSPVSQ 2317
Cdd:PHA03378   740 APGRARPPAAAPGRARPpaaAPGRARPPAAAPGApTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTS--MQLMPRAAPGQ 817
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2318 RNADSYFQQPETPRLVKNDtyaqQPNIPKPvlSDPYSQPPGTPRPGVGPEVFNRPVarTGPVSQDPFSSP-QVTMQENFV 2396
Cdd:PHA03378   818 QGPTKQILRQLLTGGVKRG----RPSLKKP--AALERQAAAGPTPSPGSGTSDKIV--QAPVFYPPVLQPiQVMRQLGSV 889
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2397 RPQTpkhsglsddgfaqpqSNPASQTPVHDPYAQ---APMTPRPQL-GDRLAREVKDQVEVGHEGSSH---------GVG 2463
Cdd:PHA03378   890 RAAA---------------ASTVTQAPTEYTGERrgvGPMHPTDIPpSKRAKTDAYVESQPPHGGQSHsfsviwenvSQG 954
                          570       580
                   ....*....|....*....|....*
gi 1658251387 2464 QFSNLQQStsnSTESQSGAQLPLGD 2488
Cdd:PHA03378   955 QQQTLECG---GTTKQERAMLGTGD 976
PHD2_NSD cd15565
PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
943-988 2.40e-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: 38.95  E-value: 2.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1658251387  943 MCVVCGSFGQGAEGrLLACSQ--CGQCYHPYCVN-IKITRVVLSKGWRC 988
Cdd:cd15565      1 SCFVCKKLGSVGGE-VFKCSVasCGKFYHEECLKkWPLTTISDSKKFRC 48
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
343-388 2.52e-03

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


Pssm-ID: 277004  Cd Length: 44  Bit Score: 38.44  E-value: 2.52e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  343 NCAVCDSPGDLLDQLFCTTCGQHYHGTCLdiGVTPLKRAGWQCPEC 388
Cdd:cd15529      1 TCTKCGDPHDEDKMMFCDQCDRGYHTFCV--GLRSIPDGRWICPLC 44
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
2231-2432 2.67e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.07  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2231 PAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRRSSPSHAMEPYPQPPGTPCPGTGERF 2310
Cdd:PRK07003   360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRG 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2311 SKSPVSQRNADSyfqqpetprlvkndtYAQQPNIPKPVLSDPYSQPPGTPRPGVGPEVFNRPVARTGPVSQDPFSSPQVT 2390
Cdd:PRK07003   440 DDAADGDAPVPA---------------KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATP 504
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1658251387 2391 MQENfvRPQTPKHSGLSDDgfAQPQSNPASQTPVHDPYAQAP 2432
Cdd:PRK07003   505 AAVP--DARAPAAASREDA--PAAAAPPAPEARPPTPAAAAP 542
ePHD_JMJD2C cd15715
Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant ...
4488-4577 2.77e-03

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: 40.71  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGPArllnldlDLWVHLNCALWSTEVYETQAGALINVELA---LRRgLSIRCVYCQR-----TGATSG 4559
Cdd:cd15715      1 CCLCNLRGGALKQTSD-------DKWAHVMCAVALPEVRFINVVERTPIDISripLQR-LKLKCIFCRNrikrvSGACIQ 72
                           90
                   ....*....|....*...
gi 1658251387 4560 CHRLRCTNVYHFTCALKA 4577
Cdd:cd15715     73 CSYGRCPASFHVTCAHAA 90
PHA02687 PHA02687
ORF061 late transcription factor VLTF-4; Provisional
26-107 2.93e-03

ORF061 late transcription factor VLTF-4; Provisional


Pssm-ID: 222918  Cd Length: 231  Bit Score: 42.69  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387   26 PVGSPTATDKRPRGRPRKDAAAATPKSRRKSRSRGKATADDEDsldgmETGETEITQEAGTKEAQGDGEGGEDSQSAEGP 105
Cdd:PHA02687    75 PESVPPAPVKTPKRRTKKKAKADKPEKSPKAVEKLCPPDDRDD-----KNEEKEPTEEAQRNEESGDAEGGASGRSPSDD 149

                   ..
gi 1658251387  106 DE 107
Cdd:PHA02687   150 DN 151
PHD1_KMT2A_like cd15506
PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
390-435 3.03e-03

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: 38.49  E-value: 3.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  390 VCQTCKNPGEDsKMLVCDTCDKGYHTFCLQPvmDSIPTNG----WRCKNC 435
Cdd:cd15506      1 LCFLCGSAGLN-ELLYCSVCCEPYHTFCLEE--AERPLNInkdnWCCRRC 47
HMG-box_HMGB_rpt2 cd21979
second high mobility group (HMG)-box found in the high mobility group protein B (HMGB) family; ...
1691-1727 3.10e-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: 3.10e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1658251387 1691 FPNLKEEFPDWStrVKQIAK----LWRKASSQERSPYVQKA 1727
Cdd:cd21979     18 RPKIKGEHPGLS--IGDVAKklgeMWNNTSAKDKQPYEKKA 56
PHD_TIF1gamma cd15624
PHD finger found in transcriptional intermediary factor 1 gamma (TIF1gamma); TIF1gamma, also ...
391-436 3.11e-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: 38.49  E-value: 3.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1658251387  391 CQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNCR 436
Cdd:cd15624      2 CAVCQNGGD---LLCCEKCPKVFHLTCHVPTLLSFPSGDWICTFCR 44
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
4488-4592 3.16e-03

Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF2. BRPF2 also termed bromodomain-containing protein 1 (BRD1), or BR140-likeprotein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a plant homeodomain (PHD) finger followed by a non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.


Pssm-ID: 277172  Cd Length: 118  Bit Score: 40.80  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTdgparllNLDLDLWVHLNCALWSTEV------YETQAGALINVELALRRglsIRCVYCQR--TGATSG 4559
Cdd:cd15702      1 CVLCPNKGGAFK-------KTDDDRWGHVVCALWIPEVgfantvFIEPIDGVRNIPPARWK---LTCYLCKQkgVGACIQ 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387 4560 CHRLRCTNVYHFTCALKA---------------QCTFFKDKTMLCHAH 4592
Cdd:cd15702     71 CHKANCYTAFHVTCAQKAglymkmepvkevtggGTTFSVRKTAYCDAH 118
PHD1_Rco1 cd15535
PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...
943-991 3.17e-03

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: 38.55  E-value: 3.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  943 MCVVCGsfgqgAEGRLLACSQCGQCYHPYCVNIKITRVVLSKG-WRCLEC 991
Cdd:cd15535      1 FCSACG-----GYGSFLCCDGCPRSFHFSCLDPPLEEDNLPDDeWFCNEC 45
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
2198-2341 3.19e-03

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: 43.87  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2198 RSDFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSKPPGTP-----RPASDSFSNSASRPGG 2272
Cdd:pfam09770  204 RAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPvtilqRPQSPQPDPAQPSIQP 283
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 2273 VDQYSPQQPSNRRSSPSHAME--PYPQPPGTPCPGTGERFSKSPVSQRnadSYFQQPETPRLVKNDTYAQQ 2341
Cdd:pfam09770  284 QAQQFHQQPPPVPVQPTQILQnpNRLSAARVGYPQNPQPGVQPAPAHQ---AHRQQGSFGRQAPIITHPQQ 351
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
468-519 3.19e-03

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 38.45  E-value: 3.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387  468 SCPLCGKPLGAEflSDHLTCQSCKRYLHLECERQAGGRTDPldREGYICTLC 519
Cdd:cd15489      1 SCIVCGKGGDLG--GELLQCDGCGKWFHADCLGPPLSSFVP--NGKWICPVC 48
PHD_BS69 cd15537
PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing ...
344-388 3.37e-03

PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a Myeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain.


Pssm-ID: 277012  Cd Length: 43  Bit Score: 38.09  E-value: 3.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  344 CAVCDSPGDLLDqlfCTTCGQHYHGTCLDIGVTPLKRAGWQCPEC 388
Cdd:cd15537      2 CFECHAPGEVLP---CSGCFRVYHSDCLSEDFRPDSTSHWTCPVC 43
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
2131-2272 3.88e-03

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 40.88  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2131 RLSDTFSQNSQNDPYAHPPLTPCTSmNDNFsnspkmmhHPQSNAFcqPMPmvrhpsrdafaqasstsrsdftqksPDPYT 2210
Cdd:pfam12868   47 DYRDYYEDPYSPSPYPPSPAGPYAS-QGQY--------YPETNYF--PPP-------------------------PGSTP 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1658251387 2211 QPPGTPRPSDPYaqppgtprPAYDP--YAQPPGTPRPFDPYSKPPGtprPASDSFSNSASRPGG 2272
Cdd:pfam12868   91 QPPVDPQPNAPP--------PPYNPadYPPPPGAAPPPQPYQYPPP---PGPDPYAPRPRRADE 143
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
344-388 4.07e-03

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


Pssm-ID: 277016 [Multi-domain]  Cd Length: 43  Bit Score: 38.09  E-value: 4.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  344 CAVCDSPGDLldqLFCTTCGQHYHGTCldiGVTPLK---RAGWQCPEC 388
Cdd:cd15541      2 CAVCQNGGEL---LCCDKCPRVFHLDC---HIPPIPefpSGEWSCSLC 43
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
988-1098 4.10e-03

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 43.43  E-value: 4.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  988 CLECTVCEACgQASDPGRLLLCDDCDISYHTYCLDppLQTVPKGSWKCKWCV-------SCTQCgATSPGVGCEWQNN-- 1058
Cdd:COG5141    193 DDICTKCTST-HNENSNAIVFCDGCEICVHQSCYG--IQFLPEGFWLCRKCIygeyqirCCSFC-PSSDGAFKQTSDGrw 268
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1658251387 1059 -YTLCApcasLTVCPICCHDYRQDELI--VQCRQCDRWMHACC 1098
Cdd:COG5141    269 gHVICA----MFNPELSFGHLLSKDPIdnIASVSSSRWKLGCL 307
PHD_JADE2 cd15680
PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger ...
390-435 4.21e-03

PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277150 [Multi-domain]  Cd Length: 46  Bit Score: 38.06  E-value: 4.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  390 VCQTCKNP-GED-SKMLVCDTCDKGYHTFCLQPVmdSIPTNGWRCKNC 435
Cdd:cd15680      1 VCDVCRSPeGEDgNEMVFCDKCNVCVHQACYGIL--KVPTGSWLCRTC 46
PHD_BRPF2 cd15677
PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar ...
993-1040 4.31e-03

PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; BRPF2, also termed bromodomain-containing protein 1 (BRD1), or BR140-like protein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277147 [Multi-domain]  Cd Length: 54  Bit Score: 38.46  E-value: 4.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1658251387  993 VCEAC--GQASDPGRLLLCDDCDISYHTYCLDPPLqtVPKGSWKCKWCVS 1040
Cdd:cd15677      3 VCCICmdGECQNSNVILFCDMCNLAVHQECYGVPY--IPEGQWLCRHCLQ 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3257-3344 4.56e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 3257 KKQYEEwLQHTQQLLKMQQKFLEEQIGAHRKSKKALSAKQRTAKKAGREFP---EEDAEQLKHVTEQQSVVQKQLEQIRK 3333
Cdd:TIGR02168  280 EEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEA 358
                           90
                   ....*....|.
gi 1658251387 3334 QQKEHAELIEE 3344
Cdd:TIGR02168  359 ELEELEAELEE 369
PHD3_KMT2D cd15597
PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
344-388 4.88e-03

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


Pssm-ID: 277072  Cd Length: 51  Bit Score: 38.09  E-value: 4.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  344 CAVCDSPGDLLDQ--LFCTTCGQHYHGTCLDIGVTPLK-RAGWQCPEC 388
Cdd:cd15597      3 CVVCGSFGRGSEGhlLACSQCSQCYHPYCVNSKITKVMlLKGWRCVEC 50
PHD_TIF1alpha cd15622
PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also ...
391-435 5.05e-03

PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also termed tripartite motif-containing protein 24 (TRIM24), or E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the TRIM/RBCC protein family. It interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta) and MOD2 (HP1gamma), as well as vertebrate Kruppel-type (C2H2) zinc finger proteins that contain transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif, and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53 and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal plant homeodomain (PHD)-Bromodomain (Bromo) region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development. TIF1-alpha 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: 277092  Cd Length: 43  Bit Score: 37.74  E-value: 5.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  391 CQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMDSIPTNGWRCKNC 435
Cdd:cd15622      2 CAVCQNGGE---LLCCEKCPKVFHLSCHVPTLMNFPSGEWICTFC 43
PHD_JADE2 cd15680
PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger ...
993-1038 5.49e-03

PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277150 [Multi-domain]  Cd Length: 46  Bit Score: 37.68  E-value: 5.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  993 VCEAC--GQASDPGRLLLCDDCDISYHTYCLDppLQTVPKGSWKCKWC 1038
Cdd:cd15680      1 VCDVCrsPEGEDGNEMVFCDKCNVCVHQACYG--ILKVPTGSWLCRTC 46
PHA03369 PHA03369
capsid maturational protease; Provisional
2191-2299 5.67e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 43.06  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2191 AQASSTSRSDFTQKSPDPYTQPPGTPRPSDPYAQPPGTPRPAYDPYAQPPGTPRPFDPYSK-PPGTPRPasdsfsnsasr 2269
Cdd:PHA03369   361 AAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPqSPGTSYG----------- 429
                           90       100       110
                   ....*....|....*....|....*....|
gi 1658251387 2270 PGGVDQYSPQQPSNRRSSPSHAMEPYPQPP 2299
Cdd:PHA03369   430 PEPVGPVPPQPTNPYVMPISMANMVYPGHP 459
PHD1_PHF12 cd15533
PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...
390-435 5.69e-03

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: 37.72  E-value: 5.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  390 VCQTCKNPGEdskMLVCDTCDKGYHTFCLQPVMD--SIPTNGWRCKNC 435
Cdd:cd15533      1 YCDSCGEGGD---LLCCDRCPASFHLQCCNPPLDeeDLPPGEWLCHRC 45
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
2149-2362 6.01e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 6.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2149 PLTPCTSMND-NFSNSPKMMHHPQSNAFCQPMPMVRHPSrDAFAQASSTSRSDFTQKSPDPytQPPGTPRPSDPYAqppg 2227
Cdd:PLN03209   370 PLSPYTAYEDlKPPTSPIPTPPSSSPASSKSVDAVAKPA-EPDVVPSPGSASNVPEVEPAQ--VEAKKTRPLSPYA---- 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2228 tprpAYDPYaQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRRSSPSHAMEPYPQPPGTPCPgTG 2307
Cdd:PLN03209   443 ----RYEDL-KPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSP-AA 516
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2308 ERFSKSPVSQRNADSYFQQPETPRLVKNDTYAQqpniPKPVLSDPYS-----QPPGTPRP 2362
Cdd:PLN03209   517 PVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQ----PKPRPLSPYTmyedlKPPTSPTP 572
PHD_BAZ2A_like cd15545
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...
944-991 6.21e-03

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: 37.68  E-value: 6.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1658251387  944 CVVCGSFGQgaEGRLLACSQCGQCYHPYCVNIKITRVvlSKG-WRCLEC 991
Cdd:cd15545      2 CQICRSGDN--EDQLLLCDGCDRGYHTYCFKPKMTNV--PEGdWFCPEC 46
PHD4_NSD3 cd15658
PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
991-1038 6.23e-03

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


Pssm-ID: 277128  Cd Length: 40  Bit Score: 37.59  E-value: 6.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1658251387  991 CTVCeacgqaSDPGRLLLCDDCDISYHTYCLDPPLqtvPKGSWKCKWC 1038
Cdd:cd15658      2 CFVC------ARGGRLLCCESCPASFHPECLSIEM---PEGCWNCNEC 40
ePHD_JMJD2 cd15675
Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
285-315 6.33e-03

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: 39.65  E-value: 6.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1658251387  285 CAYCKRL-------GASIKCCQEECSRSYHYPCAAAAG 315
Cdd:cd15675     56 CIYCSKItksmshmGACIQCSTGKCTTSFHVTCAHAAG 93
PHD_TIF1alpha cd15622
PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also ...
997-1038 6.45e-03

PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also termed tripartite motif-containing protein 24 (TRIM24), or E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the TRIM/RBCC protein family. It interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta) and MOD2 (HP1gamma), as well as vertebrate Kruppel-type (C2H2) zinc finger proteins that contain transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif, and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53 and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal plant homeodomain (PHD)-Bromodomain (Bromo) region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development. TIF1-alpha 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: 277092  Cd Length: 43  Bit Score: 37.35  E-value: 6.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1658251387  997 CGQASDPGRLLLCDDCDISYHTYCLDPPLQTVPKGSWKCKWC 1038
Cdd:cd15622      2 CAVCQNGGELLCCEKCPKVFHLSCHVPTLMNFPSGEWICTFC 43
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
4861-4974 6.59e-03

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


Pssm-ID: 380928  Cd Length: 130  Bit Score: 39.98  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4861 VYLARSRIQ--GLGLYAARDIEKYTMVIEYIGT-IIRNEVANRKEkmyeSQNRgvYMFRIDSEHVIDAtitggPARY--- 4934
Cdd:cd10530      9 VYVAESLIPsaGEGLFAKVAVGPNTVMSFYNGVrITHQEVDSRDW----SLNG--NTISLDEETVIDV-----PEPYnsv 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1658251387 4935 ----------INHSCAPNCVAEVVTFEK-GHKIIISSNRKIQRGEELCYDY 4974
Cdd:cd10530     78 skycaslghkANHSFTPNCIYDPFVHPRfGPIKCIRTLRAVEAGEELTVAY 128
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
4935-4974 6.70e-03

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; 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. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation.


Pssm-ID: 380924 [Multi-domain]  Cd Length: 210  Bit Score: 41.25  E-value: 6.70e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1658251387 4935 INHSCAPNCVaevVTFEKGhKIIISSNRKIQRGEELCYDY 4974
Cdd:cd10526    146 VNHDCWPNCT---VIFNNG-RIELRALGKISEGDELTVSY 181
PHA03247 PHA03247
large tegument protein UL36; Provisional
1991-2314 6.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 6.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1991 PSSGHESFGSPTSASVDPYAKPPDTPRPAVTADPFVKPMGPPKAGivlesqgrHMPASVIGDAFARPShraeayqrmshn 2070
Cdd:PHA03247   247 PLRGDIAAPAPPPVVGEGADRAPETARGATGPPPPPEAAAPNGAA--------APPDGVWGAALAGAP------------ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2071 kmvLSDPYSKPLLTPIPGSN---ESGSVPLFKAPMPPPHPQDLYNSTPSIGRRnsvdsferptrlsdtfsqnsqndpyah 2147
Cdd:PHA03247   307 ---LALPAPPDPPPPAPAGDaeeEDDEDGAMEVVSPLPRPRQHYPLGFPKRRR--------------------------- 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2148 PPLTPCTSMNDNFSNSpkmmHHPQSnafcqpMPMVRHPSRDAFAQASSTSRSDFTQKSPDPYTQPPGTPRPSDPYAQPPG 2227
Cdd:PHA03247   357 PTWTPPSSLEDLSAGR----HHPKR------ASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVPASVPTPAPTPVPAS 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2228 TPRPAYDPY--AQPPGTPRPfdpysKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNRRsspshamepypqPPGTPCPG 2305
Cdd:PHA03247   427 APPPPATPLpsAEPGSDDGP-----APPPERQPPAPATEPAPDDPDDATRKALDALRERR------------PPEPPGAD 489

                   ....*....
gi 1658251387 2306 TGERFSKSP 2314
Cdd:PHA03247   490 LAELLGRHP 498
PHA03369 PHA03369
capsid maturational protease; Provisional
2217-2302 6.77e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 42.68  E-value: 6.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2217 RPSDPYAQPP--GTPRPAYDPYAQPPGTPRPFDPYSKPPGTPRPASDSFSNSASRPGGVDQYSPQQPSNrrSSPSHAMEP 2294
Cdd:PHA03369   358 RVLAAAAKVAviAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSPGT--SYGPEPVGP 435

                   ....*...
gi 1658251387 2295 YPQPPGTP 2302
Cdd:PHA03369   436 VPPQPTNP 443
PHA03377 PHA03377
EBNA-3C; Provisional
2182-2483 6.83e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 43.12  E-value: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2182 VRHPSRDAFAQASSTSRSDFTQKSPDPYTQPP---GTPRPSDPYAQPPGT-PRPAYDPYAQPPG---------------- 2241
Cdd:PHA03377   526 VTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPsdrGPPKASPPVMAPPSTgPRVMATPSTGPRDmappstgprqqakckd 605
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2242 -----TPRPFDPYSKPPGTPRP------------------ASDSF-SNSASRPGGVDQyspQQPSNRRSSPSHAMEPYPQ 2297
Cdd:PHA03377   606 gppasGPHEKQPPSSAPRDMAPsvvrmflrerlleqstgpKPKSFwEMRAGRDGSGIQ---QEPSSRRQPATQSTPPRPS 682
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2298 -----------PPGTPCPGTGERfsKSPVSQRNADSYFQQP--ETPRlVKNDTYAQQPNIPKPVLSDPYS---QPPGT-- 2359
Cdd:PHA03377   683 wlpsvfvlpsvDAGRAQPSEESH--LSSMSPTQPISHEEQPryEDPD-DPLDLSLHPDQAPPPSHQAPYSgheEPQAQqa 759
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2360 -------PRPGVGPEV-FNRPVARTGPVSQDP-FSSPQVTmqenfvRPQTPKHsglsddgfaQPQSNPASQTPVH----D 2426
Cdd:PHA03377   760 pypgywePRPPQAPYLgYQEPQAQGVQVSSYPgYAGPWGL------RAQHPRY---------RHSWAYWSQYPGHghpqG 824
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1658251387 2427 PYAQAPMTPRPQLgDRLAREVKDQVEvghegsshgvgQFSNLQQSTSNSTESQSGAQ 2483
Cdd:PHA03377   825 PWAPRPPHLPPQW-DGSAGHGQDQVS-----------QFPHLQSETGPPRLQLSQVP 869
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
246-330 6.94e-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: 39.50  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387  246 TGQCCAHQRCAVWSRGV---CRGEGTSLLNVDKAIDSGSTESCAYCK-RLGASIKCCQEECSRSYHYPCAAAAG------ 315
Cdd:cd15707     16 SGTKWAHVSCALWIPEVsigCVEKMEPITKISSIPASRWALICVLCReRTGACIQCSVKTCKTAYHVTCGFQHGlemkti 95
                           90
                   ....*....|....*...
gi 1658251387  316 ---TFQDFRKLTLLCPKH 330
Cdd:cd15707     96 ldeESEDGVKLRSYCQKH 113
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
1909-2083 6.96e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.74  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1909 PPTGTRLTEACSQGQASQPQSPQMFSTGTASSSSRPSSPWDPYAKM-VGTPRP-------PPigssTPRRNSTESCSAPR 1980
Cdd:PRK14959   380 APSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPApSAAPSPrvpwddaPP----APPRSGIPPRPAPR 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 1981 LPSEQQERGRPSSGHESFGSPTSASvDPYAKPPDTPRPAVTADPFVK------PMGPPKAGIVLESQGRHmpasviGDAF 2054
Cdd:PRK14959   456 MPEASPVPGAPDSVASASDAPPTLG-DPSDTAEHTPSGPRTWDGFLEfcqgrnGQGGRLATVLRQATPEH------ADGR 528
                          170       180       190
                   ....*....|....*....|....*....|
gi 1658251387 2055 ARPSHRAEA-YQRmshnkmvLSDPYSKPLL 2083
Cdd:PRK14959   529 LRLATMSSVqYER-------LTDAATETTL 551
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
390-432 7.43e-03

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 37.31  E-value: 7.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  390 VCQTCKNPGEdskMLVCD--TCDKGYHTFCLQpvMDSIPTNGWRC 432
Cdd:cd15568      1 ECFRCGDGGD---LVLCDfkGCPKVYHLSCLG--LEKPPGGKWIC 40
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
246-317 7.60e-03

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 42.66  E-value: 7.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1658251387  246 TGQCCaHQRCAVWSRGVCRGEGTSLLNVD--KAIDSGSTES-CAYCK-RLGASIKCCQEECSRSYHYPCAAAAGTF 317
Cdd:COG5141    265 DGRWG-HVICAMFNPELSFGHLLSKDPIDniASVSSSRWKLgCLICKeFGGTCIQCSYFNCTRAYHVTCARRAGYF 339
PHD1_DPF3 cd15692
PHD finger 1 found in D4, zinc and double PHD fingers family 3 (DPF3); DPF3, also termed ...
953-991 7.69e-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: 37.74  E-value: 7.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1658251387  953 GAEGRLLACSQCGQCYHPYCVN--IKITRVVLSKGWRCLEC 991
Cdd:cd15692     16 GRPEELVSCADCGRSGHPTCLQftVNMTEAVKTYQWQCIEC 56
PHD_SP110_140 cd15626
PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family ...
994-1038 7.85e-03

PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family includes nuclear body proteins SP100, SP140, and similar proteins. Sp110, also termed interferon-induced protein 41/75, or speckled 110 kDa, or transcriptional coactivator 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. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population. Sp110 contains a Sp100-like domain, a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD). SP140, also termed lymphoid-restricted homolog of Sp100 (LYSp100), or nuclear autoantigen Sp-140, or speckled 140 kDa, 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's viral infectivity factor (Vif) protein. Sp140 contains a nuclear localization signal, a dimerization domain (HSR or CARD domain), a SAND domain, a PHD finger, and a BRD.


Pssm-ID: 277096  Cd Length: 42  Bit Score: 37.02  E-value: 7.85e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387  994 CEACGQAsdpGRLLLCDDCDISYHTYCLDPPLQtVPKGSWKCKWC 1038
Cdd:cd15626      2 CEVCGQE---GKLFCCCTCSRVFHEDCHIPPVE-AQRSPWSCTFC 42
PRK05901 PRK05901
RNA polymerase sigma factor; Provisional
2778-2900 8.06e-03

RNA polymerase sigma factor; Provisional


Pssm-ID: 235640 [Multi-domain]  Cd Length: 509  Bit Score: 42.29  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 2778 TPADQPEDIAVNTEgIEEKLDTDDSAVKDLEDVEVKDLDDEDLENLNLDPDSTKELDLETSDLHLDDFLKSGKFDIIAYT 2857
Cdd:PRK05901    86 AAAKAPAKKKLKDE-LDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDDDD 164
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1658251387 2858 DPDLDLGDK--KDMFNEELDLSDPIDDQSEASDLQKALSEKRNAS 2900
Cdd:PRK05901   165 VDDEDEEKKeaKELEKLSDDDDFVWDEDDSEALRQARKDAKLTAT 209
PHD4_KMT2C cd15596
PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
388-435 9.08e-03

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: 37.69  E-value: 9.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1658251387  388 CKVCQTCKNpGEDSKMLVCDTCDKGYHTFCLQ-PVMDSIPTNGWRCKNC 435
Cdd:cd15596      9 CVVCGSFGQ-GAEGRLLACSQCGQCYHPYCVSiKITKVVLSKGWRCLEC 56
ePHD_JMJD2A cd15713
Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...
4488-4577 9.40e-03

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: 39.19  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658251387 4488 CCFCHEEGDGLTDGparllnlDLDLWVHLNCALWSTEVYETQAGALINVELA---LRRgLSIRCVYCQR-----TGATSG 4559
Cdd:cd15713      1 CCLCSLRGGALQRA-------NDDKWVHVMCAVAVLEARFVNIAERSPVDVSkipLQR-FKLKCIFCKKrrkrtAGCCVQ 72
                           90
                   ....*....|....*...
gi 1658251387 4560 CHRLRCTNVYHFTCALKA 4577
Cdd:cd15713     73 CSHGRCPTSFHASCAQAA 90
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
1070-1120 9.47e-03

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 37.14  E-value: 9.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1658251387 1070 VCPICC-HDYRQDELIVQCRQCDRWMHACCQNLNSDEEVENvadDGFECAMC 1120
Cdd:cd15517      1 VCGICNlETAAVDELWVQCDGCDKWFHQFCLGLSNERYADE---DKFKCPNC 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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