NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564355920|ref|XP_006240140|]
View 

G2/M phase-specific E3 ubiquitin-protein ligase isoform X1 [Rattus norvegicus]

Protein Classification

G2/M phase-specific E3 ubiquitin-protein ligase( domain architecture ID 11609341)

G2/M phase-specific E3 ubiquitin-protein ligase (G2E3) acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates

CATH:  3.30.40.10|3.90.1750.10|3.30.2410.10|3.30.2160.10
EC:  2.3.2.26
Gene Symbol:  G2E3
Gene Ontology:  GO:0004842|GO:0006915|GO:0008270|GO:0016567
PubMed:  16297627|21514168|7701562|29016349|32265230
SCOP:  4003778|4002196

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 14-127 5.43e-59

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: 194.39  E-value: 5.43e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKktCEKWNFSVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15669    1 CVLCGRSDDDPDKYGEK--LQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564355920  94 VVPQCKRSYHLPCGLQKECIFQFTDNFASFCWKH 127
Cdd:cd15669   79 AVKGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112
PHD_PHF7_G2E3_like cd15496
PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ...
 232-285 1.68e-27

PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); PHF7, also termed testis development protein NYD-SP6, is a testis-specific plant homeodomain (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 canonical Cys4HisCys3 PHD finger and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, 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. This model corresponds to the Cys4HisCys3 canonical PHD finger.


:

Pssm-ID: 276971  Cd Length: 54  Bit Score: 105.19  E-value: 1.68e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564355920 232 RCDVRRCHCKEGREYNEPNSKWEIKRCQCCGSSGTHLACSSLQSWEKNWECLDC 285
Cdd:cd15496    1 RCDARKCLCPQGREYNEPEGKWELVLCQSCGSRGTHRACSSLRSWEQSWECVEC 54
HECTc super family cl27008
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 365-688 7.67e-13

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


The actual alignment was detected with superfamily member cd00078:

Pssm-ID: 474882 [Multi-domain]  Cd Length: 352  Bit Score: 70.29  E-value: 7.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 365 INKANVWRSAVEQFQSQK-FNPSYSIEVVYVNdndEVGSKHPGSKQEFLSHLMHHLENSSV--FE--GSLAKNLSLNSQA 439
Cdd:cd00078    5 VRRDRILEDALRQLSKVSsSDLKKVLEVEFVG---EEGIDAGGVTREFFTLVSKELFNPSYglFRytPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 440 ----VKENLYYEAGKMLAISLVHGGPSPGFFSETLFKCLAygpeNALPTLDDVSDLDVA-----QIIIKIDTAADLNILK 510
Cdd:cd00078   82 fadeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL----GKPLSLEDLEELDPElykslKELLDNDGDEDDLELT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 511 SVINEYYNYLEFSG---CLR---LMTTLSDKYMLVKDILFYQVIKRVKAPFESFKQGLKTLGVLEKIQA-YPEAFYNILC 583
Cdd:cd00078  158 FTIELDSSFGGAVTvelKPGgrdIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLfTPEELELLIC 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 584 HKPESlsakNLSDL--FTIHKLPDVKTSR----FWnsylQAVEdgksATTLED---ILHFATGCSSVPPTGFK---PAPS 651
Cdd:cd00078  238 GSEDI----DLEDLkkNTEYKGGYSSDSPtiqwFW----EVLE----SFTNEErkkFLQFVTGSSRLPVGGFAdlnPKFT 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 564355920 652 IECLHGD---FPVANKCNNCLALPVTNTYEEFQENMDFAI 688
Cdd:cd00078  306 IRRVGSPddrLPTAHTCFNLLKLPPYSSKEILREKLLYAI 345
 
Name Accession Description Interval E-value
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 14-127 5.43e-59

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: 194.39  E-value: 5.43e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKktCEKWNFSVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15669    1 CVLCGRSDDDPDKYGEK--LQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564355920  94 VVPQCKRSYHLPCGLQKECIFQFTDNFASFCWKH 127
Cdd:cd15669   79 AVKGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112
PHD_PHF7_G2E3_like cd15496
PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ...
 232-285 1.68e-27

PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); PHF7, also termed testis development protein NYD-SP6, is a testis-specific plant homeodomain (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 canonical Cys4HisCys3 PHD finger and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, 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. This model corresponds to the Cys4HisCys3 canonical PHD finger.


Pssm-ID: 276971  Cd Length: 54  Bit Score: 105.19  E-value: 1.68e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564355920 232 RCDVRRCHCKEGREYNEPNSKWEIKRCQCCGSSGTHLACSSLQSWEKNWECLDC 285
Cdd:cd15496    1 RCDARKCLCPQGREYNEPEGKWELVLCQSCGSRGTHRACSSLRSWEQSWECVEC 54
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 41-127 6.50e-26

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: 101.64  E-value: 6.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   41 HYYCLLMSSGIWQRGKEEEGvygFLIEDIRKEVNRASKLKCTVCKKN-GASIGCVVPQCKRSYHLPCGLQKECIFQFTDN 119
Cdd:pfam13771   1 HVVCALWSPELVQRGNDSMG---FPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDED 77

                          90
                  ....*....|.
gi 564355920  120 ---FASFCWKH 127
Cdd:pfam13771  78 ngtFKSYCKKH 88
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 365-688 7.67e-13

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 70.29  E-value: 7.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 365 INKANVWRSAVEQFQSQK-FNPSYSIEVVYVNdndEVGSKHPGSKQEFLSHLMHHLENSSV--FE--GSLAKNLSLNSQA 439
Cdd:cd00078    5 VRRDRILEDALRQLSKVSsSDLKKVLEVEFVG---EEGIDAGGVTREFFTLVSKELFNPSYglFRytPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 440 ----VKENLYYEAGKMLAISLVHGGPSPGFFSETLFKCLAygpeNALPTLDDVSDLDVA-----QIIIKIDTAADLNILK 510
Cdd:cd00078   82 fadeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL----GKPLSLEDLEELDPElykslKELLDNDGDEDDLELT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 511 SVINEYYNYLEFSG---CLR---LMTTLSDKYMLVKDILFYQVIKRVKAPFESFKQGLKTLGVLEKIQA-YPEAFYNILC 583
Cdd:cd00078  158 FTIELDSSFGGAVTvelKPGgrdIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLfTPEELELLIC 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 584 HKPESlsakNLSDL--FTIHKLPDVKTSR----FWnsylQAVEdgksATTLED---ILHFATGCSSVPPTGFK---PAPS 651
Cdd:cd00078  238 GSEDI----DLEDLkkNTEYKGGYSSDSPtiqwFW----EVLE----SFTNEErkkFLQFVTGSSRLPVGGFAdlnPKFT 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 564355920 652 IECLHGD---FPVANKCNNCLALPVTNTYEEFQENMDFAI 688
Cdd:cd00078  306 IRRVGSPddrLPTAHTCFNLLKLPPYSSKEILREKLLYAI 345
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 441-691 9.57e-12

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 66.48  E-value: 9.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  441 KENLYYEAGKMLAISLVHGGPSPGFFSETLFKCLAygpeNALPTLDDVSDLD--VAQIIIKI-----DTAADLNIlksvi 513
Cdd:pfam00632  39 LLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL----GEPLTLEDLESIDpeLYKSLKSLlnmdnDDDEDLGL----- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  514 NEYYNYLEFSGCLRL-------MTTLSDKYMLVKDILFYQVIKRVKAPFESFKQGLKTLGVLEKIQAY-PEAFYNILCHK 585
Cdd:pfam00632 110 TFTIPVFGESKTIELipngrniPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFtPEELELLICGS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  586 PEsLSAKNLSDlFTIHKLPDVKTSR----FWNSYLQAVEDGKSAttledILHFATGCSSVPPTGFKPAPS--IECLHGD- 658
Cdd:pfam00632 190 PE-IDVEDLKK-NTEYDGGYTKNSPtiqwFWEILEEFSPEQRRL-----FLKFVTGSSRLPVGGFKSLPKftIVRKGGDd 262

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 564355920  659 ---FPVANKCNNCLALPVTNTYEEFQENMDFAIRDS 691
Cdd:pfam00632 263 ddrLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG 298
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 388-689 1.48e-11

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 66.10  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   388 SIEVVYVNdndEVGSKHPGSKQEFLSHLMHHLENSSV--FEGSLAKNL----SLNSQAVKENL--YYEAGKMLAISLVHG 459
Cdd:smart00119   6 VLEIEFEG---EEGLDGGGVTREFFFLLSKELFNPDYglFRYSPNDYLlypnPRSGFANEEHLsyFRFIGRVLGKALYDN 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   460 GPSPGFFSETLFKCLAygpeNALPTLDDVSDLD------VAQIIIKIDT--AADLNILKSVINEYYNY----LEFSGClR 527
Cdd:smart00119  83 RLLDLFFARPFYKKLL----GKPVTLHDLESLDpelyksLKWLLLNNDTseELDLTFSIVLTSEFGQVkvveLKPGGS-N 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   528 LMTTLSDKYMLVKDILFYQVIKRVKAPFESFKQGLKTLGVLEKIQAY-PEAFYNILCHKPESlsakNLSDL--FTIHKL- 603
Cdd:smart00119 158 IPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFdPEELELLICGSPEI----DVDDLksNTEYKGg 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   604 -----PDVKtsRFWnsylQAVEdgksATTLED---ILHFATGCSSVPPTGFKP-APSIeCLHGD------FPVANKCNNC 668
Cdd:smart00119 234 ysansQTIK--WFW----EVVE----SFTNEErrkLLQFVTGSSRLPVGGFAAlSPKF-TIRKAgsdderLPTAHTCFNR 302

                          330       340
                   ....*....|....*....|.
gi 564355920   669 LALPVTNTYEEFQENMDFAIR 689
Cdd:smart00119 303 LKLPPYSSKEILREKLLLAIN 323
 
Name Accession Description Interval E-value
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 14-127 5.43e-59

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: 194.39  E-value: 5.43e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKktCEKWNFSVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15669    1 CVLCGRSDDDPDKYGEK--LQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564355920  94 VVPQCKRSYHLPCGLQKECIFQFTDNFASFCWKH 127
Cdd:cd15669   79 AVKGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112
PHD_PHF7_G2E3_like cd15496
PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ...
 232-285 1.68e-27

PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); PHF7, also termed testis development protein NYD-SP6, is a testis-specific plant homeodomain (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 canonical Cys4HisCys3 PHD finger and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, 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. This model corresponds to the Cys4HisCys3 canonical PHD finger.


Pssm-ID: 276971  Cd Length: 54  Bit Score: 105.19  E-value: 1.68e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564355920 232 RCDVRRCHCKEGREYNEPNSKWEIKRCQCCGSSGTHLACSSLQSWEKNWECLDC 285
Cdd:cd15496    1 RCDARKCLCPQGREYNEPEGKWELVLCQSCGSRGTHRACSSLRSWEQSWECVEC 54
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 41-127 6.50e-26

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: 101.64  E-value: 6.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   41 HYYCLLMSSGIWQRGKEEEGvygFLIEDIRKEVNRASKLKCTVCKKN-GASIGCVVPQCKRSYHLPCGLQKECIFQFTDN 119
Cdd:pfam13771   1 HVVCALWSPELVQRGNDSMG---FPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDED 77

                          90
                  ....*....|.
gi 564355920  120 ---FASFCWKH 127
Cdd:pfam13771  78 ngtFKSYCKKH 88
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
 14-127 5.93e-24

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: 97.08  E-value: 5.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDcpNKYGEKKTCEKWNFSVHYYCLLMSSGIWQRGKEEEGVY-GFLIEDIRKEVNRASKLKCTVCKKNGASIG 92
Cdd:cd15673    1 CGFCKSGEE--NKETGGKLASGEKIAAHHNCMLFSSGLVQYVSPNENDFgGFDIEDVKKEIKRGRKLKCNLCKKTGATIG 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564355920  93 CVVPQCKRSYHLPCGLQKECIFQFTDN---FASFCWKH 127
Cdd:cd15673   79 CDVKQCKKTYHYHCAKKDDAKIIERNSqgiYRVYCKNH 116
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 14-127 1.63e-21

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: 89.95  E-value: 1.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKKTcEKWNFSVHYYCLLMSSGIWQRGKEEEGVygfliEDIRKEVNRASKLKCTVCKKN-GASIG 92
Cdd:cd15571    1 CALCPRSGGALKGGGALKT-TSDGLWVHVVCALWSPEVYFDDGTLLEV-----EGVSKIPKRRKKLKCSICGKRgGACIQ 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564355920  93 CVVPQCKRSYHLPCGLQKECIFQFT---DNFASFCWKH 127
Cdd:cd15571   75 CSYPGCPRSFHVSCAIRAGCLFEFEdgpGNFVVYCPKH 112
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 14-127 5.22e-19

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: 83.09  E-value: 5.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDcpNKYGEKKTCEKWNFSVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15710    1 CGFCRSNRE--KECGQLLISENQKVAAHHKCMLFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGC 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564355920  94 VVPQCKRSYHLPCGLQKECifQFTDN-----FASFCWKH 127
Cdd:cd15710   79 DVKTCHRTYHYYCALHDKA--QIRENpsqgiYMIYCRKH 115
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 14-127 7.54e-14

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: 68.20  E-value: 7.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRK-NDDCPNKYGEKKTC--EKWnfsVHYYCLLMSSGIWQrgkEEEGVygflIEDIRKEVNRASKLKCTVCKKNGAS 90
Cdd:cd15664    1 CALCGVyGDDEPNDAGRLLYCgqDEW---VHINCALWSAEVFE---EDDGS----LQNVHSAVSRGRMMKCELCGKPGAT 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564355920  91 IGCVVPQCKRSYHLPCGLQKECIFQftDNFASFCWKH 127
Cdd:cd15664   71 VGCCLKSCPANYHFMCARKAECVFQ--DDKKVFCPAH 105
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 14-126 4.33e-13

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: 66.26  E-value: 4.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKKTCEKWNFSVHYYCLLMSSGIWQRGKEEEGVYG-FLIEDIRKEVNRASKLKCTVCKKNGASIG 92
Cdd:cd15711    1 CGFCHAGEEENETRGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGdFDIKTVIQEIKRGKRMKCTLCSQLGATIG 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564355920  93 CVVPQCKRSYHLPCGLQKECifQFTDNFASFCWK 126
Cdd:cd15711   81 CEIKACVKTYHYHCGVQDKA--KYIENMSRGIYK 112
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 14-127 4.90e-13

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: 65.79  E-value: 4.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNddcPNKYGEKKTC----EKWnfsVHYYCLLMSSGIWQRGKEeegVYGfLIEDIRKevnrASKLKCTVCKKNGA 89
Cdd:cd15668    1 CVFCKRG---PHYKGLGDLFgpyyEVW---VHEDCAVWAPGVYLVGGK---LYG-LEEAVWV----AKQSVCSSCQQTGA 66

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564355920  90 SIGCVVPQCKRSYHLPCGLQKECIFQfTDNFASFCWKH 127
Cdd:cd15668   67 TIGCLHKGCKAKYHYPCAVESGCQLD-EENFSLLCPKH 103
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 365-688 7.67e-13

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 70.29  E-value: 7.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 365 INKANVWRSAVEQFQSQK-FNPSYSIEVVYVNdndEVGSKHPGSKQEFLSHLMHHLENSSV--FE--GSLAKNLSLNSQA 439
Cdd:cd00078    5 VRRDRILEDALRQLSKVSsSDLKKVLEVEFVG---EEGIDAGGVTREFFTLVSKELFNPSYglFRytPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 440 ----VKENLYYEAGKMLAISLVHGGPSPGFFSETLFKCLAygpeNALPTLDDVSDLDVA-----QIIIKIDTAADLNILK 510
Cdd:cd00078   82 fadeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL----GKPLSLEDLEELDPElykslKELLDNDGDEDDLELT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 511 SVINEYYNYLEFSG---CLR---LMTTLSDKYMLVKDILFYQVIKRVKAPFESFKQGLKTLGVLEKIQA-YPEAFYNILC 583
Cdd:cd00078  158 FTIELDSSFGGAVTvelKPGgrdIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLfTPEELELLIC 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920 584 HKPESlsakNLSDL--FTIHKLPDVKTSR----FWnsylQAVEdgksATTLED---ILHFATGCSSVPPTGFK---PAPS 651
Cdd:cd00078  238 GSEDI----DLEDLkkNTEYKGGYSSDSPtiqwFW----EVLE----SFTNEErkkFLQFVTGSSRLPVGGFAdlnPKFT 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 564355920 652 IECLHGD---FPVANKCNNCLALPVTNTYEEFQENMDFAI 688
Cdd:cd00078  306 IRRVGSPddrLPTAHTCFNLLKLPPYSSKEILREKLLYAI 345
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 14-127 1.20e-12

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: 64.92  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYgekkTCEKWNFSVHYYCLLMSSGIWQRGKE--EEGVYGFLIEDIRKEVNRASKLKCTVCKKNGASI 91
Cdd:cd15712    1 CAFCPKGEEYSIMY----FAQEQNIAAHQNCLLYSSGFVESEEYnpLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564355920  92 GCVVPQCKRSYHLPCGLQKECIFQfTDN----FASFCWKH 127
Cdd:cd15712   77 GCEERACRRSYHYFCALCDDAAIE-TDEvrgiYRVFCQKH 115
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 14-127 1.41e-12

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: 64.24  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFC-RKNDDCPNKYGE--KKTCEKWnfsVHYYCLLMSSGIWqrgkeeEGVYGFLIeDIRKEVNRASKLKCTVCKKNGAS 90
Cdd:cd15666    1 CVLCgGEGDGDTDGPGRllNLDVDKW---VHLNCALWSYEVY------ETQNGALM-NVEEALRRALTTTCSHCGRTGAT 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564355920  91 IGCVVPQCKRSYHLPCGLQKECIFqFTDNfASFCWKH 127
Cdd:cd15666   71 VPCFKPRCANVYHLPCAIKDGCMF-FKDK-TMLCPSH 105
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 441-691 9.57e-12

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 66.48  E-value: 9.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  441 KENLYYEAGKMLAISLVHGGPSPGFFSETLFKCLAygpeNALPTLDDVSDLD--VAQIIIKI-----DTAADLNIlksvi 513
Cdd:pfam00632  39 LLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLL----GEPLTLEDLESIDpeLYKSLKSLlnmdnDDDEDLGL----- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  514 NEYYNYLEFSGCLRL-------MTTLSDKYMLVKDILFYQVIKRVKAPFESFKQGLKTLGVLEKIQAY-PEAFYNILCHK 585
Cdd:pfam00632 110 TFTIPVFGESKTIELipngrniPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFtPEELELLICGS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  586 PEsLSAKNLSDlFTIHKLPDVKTSR----FWNSYLQAVEDGKSAttledILHFATGCSSVPPTGFKPAPS--IECLHGD- 658
Cdd:pfam00632 190 PE-IDVEDLKK-NTEYDGGYTKNSPtiqwFWEILEEFSPEQRRL-----FLKFVTGSSRLPVGGFKSLPKftIVRKGGDd 262

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 564355920  659 ---FPVANKCNNCLALPVTNTYEEFQENMDFAIRDS 691
Cdd:pfam00632 263 ddrLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG 298
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 388-689 1.48e-11

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 66.10  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   388 SIEVVYVNdndEVGSKHPGSKQEFLSHLMHHLENSSV--FEGSLAKNL----SLNSQAVKENL--YYEAGKMLAISLVHG 459
Cdd:smart00119   6 VLEIEFEG---EEGLDGGGVTREFFFLLSKELFNPDYglFRYSPNDYLlypnPRSGFANEEHLsyFRFIGRVLGKALYDN 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   460 GPSPGFFSETLFKCLAygpeNALPTLDDVSDLD------VAQIIIKIDT--AADLNILKSVINEYYNY----LEFSGClR 527
Cdd:smart00119  83 RLLDLFFARPFYKKLL----GKPVTLHDLESLDpelyksLKWLLLNNDTseELDLTFSIVLTSEFGQVkvveLKPGGS-N 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   528 LMTTLSDKYMLVKDILFYQVIKRVKAPFESFKQGLKTLGVLEKIQAY-PEAFYNILCHKPESlsakNLSDL--FTIHKL- 603
Cdd:smart00119 158 IPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFdPEELELLICGSPEI----DVDDLksNTEYKGg 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920   604 -----PDVKtsRFWnsylQAVEdgksATTLED---ILHFATGCSSVPPTGFKP-APSIeCLHGD------FPVANKCNNC 668
Cdd:smart00119 234 ysansQTIK--WFW----EVVE----SFTNEErrkLLQFVTGSSRLPVGGFAAlSPKF-TIRKAgsdderLPTAHTCFNR 302

                          330       340
                   ....*....|....*....|.
gi 564355920   669 LALPVTNTYEEFQENMDFAIR 689
Cdd:smart00119 303 LKLPPYSSKEILREKLLLAIN 323
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 38-127 2.80e-10

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: 57.33  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  38 FSVHYYCLLMSSGIWQrgKEEEgvygfLIEDIRKEVNRASKLKCTVCKKNGASIGCVVPQCKRSYHLPCGLQKECiFQFT 117
Cdd:cd15665    9 VYAHHCCAAWSEGVCQ--TEDG-----ALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGC-FQDI 80

                         90
                 ....*....|
gi 564355920 118 DNFASFCWKH 127
Cdd:cd15665   81 KTLTLFCPEH 90
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 14-127 1.59e-09

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: 55.82  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKKTCEKWNFSVHYYCLLMSSGIWQrgkEEEGVygflIEDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15694    1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFE---ENDGS----LKNVHAAVARGRQMRCEHCQKIGATVGC 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564355920  94 VVPQCKRSYHLPCGLQKECIFQftDNFASFCWKH 127
Cdd:cd15694   74 CLSACLSNFHFMCARASRCCFQ--DDKKVFCQKH 105
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 41-128 9.73e-09

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: 53.85  E-value: 9.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  41 HYYCLLMSSGIWQrgkEEEGVygflIEDIRKEVNRASKLKCTVCKKNGASIGCVVPQCKRSYHLPCGLQKECIfqFTDNF 120
Cdd:cd15693   30 HVNCALWSAEVFE---DDDGS----LKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCV--FLEDK 100


                 ....*...
gi 564355920 121 ASFCWKHR 128
Cdd:cd15693  101 KVYCQRHK 108
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
 36-127 1.03e-08

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: 53.38  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  36 WNFSVHYYCLLMSSGIWQRGKEeegVYGfliedIRKEVNRASKLKCTVCKKNGASIGCVVPQCKRSYHLPCGLQKECIFQ 115
Cdd:cd15699   21 YEFWVHEGCILWANGIYLVCGR---LYG-----LQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLN 92

                         90
                 ....*....|..
gi 564355920 116 fTDNFASFCWKH 127
Cdd:cd15699   93 -EENFSVRCPKH 103
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 34-127 4.97e-07

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: 48.72  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  34 EKWnfsVHYYCLLMSSGIWQRGKEeegVYGfliedIRKEVNRASKLKCTVCKKNGASIGCVVPQCKRSYHLPCGLQKECI 113
Cdd:cd15700   23 EHW---VHEACAVWTTGVYLVAGK---LFG-----LQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCL 91

                         90
                 ....*....|....
gi 564355920 114 FQfTDNFASFCWKH 127
Cdd:cd15700   92 FE-EENFSLRCPKH 104
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 79-127 1.02e-05

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


Pssm-ID: 277141  Cd Length: 112  Bit Score: 45.13  E-value: 1.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564355920  79 LKCTVCK-KNGASIGCVVPQCKRSYHLPCGLQ-----KECIFQFTDN--FASFCWKH 127
Cdd:cd15671   56 LVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQhglemKTILEDEDDEvkFKSYCPKH 112
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 14-128 1.16e-05

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: 44.66  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKKTCEKWNFSVHYYCLLMSSGIWQrgkeeegVYGFLIEDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15698    1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYE-------TQGGALMNVEVALHRGLLTKCSLCQKTGATNSC 73

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564355920  94 VVPQCKRSYHLPCGLQKECIFqFTDNfASFCWKHR 128
Cdd:cd15698   74 NRLRCPNVYHFACAIRAKCMF-FKDK-TMLCPMHK 106
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 14-114 2.01e-05

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: 43.88  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCPNKYGEKKTCEKWNFSVHYYCLLMSSGIWqrgkeeEGVYGFLIeDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15697    1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVY------ETQAGALI-NVELALRRGLQMKCVFCHKTGATSGC 73

                         90       100
                 ....*....|....*....|.
gi 564355920  94 VVPQCKRSYHLPCGLQKECIF 114
Cdd:cd15697   74 HRLRCTNVYHFTCAIKAQCMF 94
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 40-106 2.05e-05

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: 43.75  E-value: 2.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564355920  40 VHYYCLLMSSGIWQRGKEEegvygflIEDIRKEVNRASKLKCTVCKKNGASIGCVVPQCKRSYHLPC 106
Cdd:cd15695   11 VHHWCAAWSAGVKQHEGDG-------LIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPC 70
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 14-106 1.04e-03

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: 38.77  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564355920  14 CVFCRKNDDCpnkygekktcekwnfsVHYYCLLMSSGIWQrGKEEegvygfLIEDIRKEVNRASKLKCTVCKKNGASIGC 93
Cdd:cd15696    1 CAFCYCGECW----------------AHLRCAEWSLGVCQ-GEEQ------LLVNVDKAVVSGSTERCAFCKHLGATIKC 57

                         90
                 ....*....|...
gi 564355920  94 VVPQCKRSYHLPC 106
Cdd:cd15696   58 CEEKCTQMYHYPC 70
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
 79-127 2.91e-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: 37.96  E-value: 2.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564355920  79 LKCTVCK-KNGASIGCVVPQCKRSYHLPCGLQ-----KECIFQFTDN---FASFCWKH 127
Cdd:cd15707   56 LICVLCReRTGACIQCSVKTCKTAYHVTCGFQhglemKTILDEESEDgvkLRSYCQKH 113
ePHD_JADE3 cd15706
Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...
 79-127 6.51e-03

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-3. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is close related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.


Pssm-ID: 277176  Cd Length: 111  Bit Score: 37.01  E-value: 6.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564355920  79 LKCTVCK-KNGASIGCVVPQCKRSYHLPC----GLQKECIFQFTD--NFASFCWKH 127
Cdd:cd15706   56 LVCSLCKlKTGACIQCSVKSCITAFHVTCafehSLEMKTILDEGDevKFKSYCLKH 111
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
68-127 7.36e-03

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 36.94  E-value: 7.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564355920   68 DIRKEVNRASKLKCTVCKKN-GASIGCVVPQCKRSYHLPCGLQKECIFQFTD----NFASFCWKH 127
Cdd:pfam13832  45 DVSRIPPERWKLKCVFCKKRsGACIQCSKGRCTTAFHVTCAQAAGVYMEPEDwpnvVVIAYCQKH 109
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH