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Conserved domains on  [gi|442617064|ref|NP_001259740|]
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PHD finger protein 7, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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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 ...
 5-116 1.86e-51

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: 170.89  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELIFGTVHVEGNMMVHRNCLYLSSNLIQRGEKKLSIMNFLKEDIEAEVNRCRLLKCCYCRRLGANIWCCK 84
Cdd:cd15669    1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442617064  85 SGCRRTFHTKCGVDNLAQNQFCDTYNSFCHQH 116
Cdd:cd15669   81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 129-183 8.74e-04

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16494:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 57  Bit Score: 37.70  E-value: 8.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442617064 129 DEECLLCAEDVVAKGErfSVVTCLYApcCRNGwFHRRCLQRYAN---SSGYFFKCPLC 183
Cdd:cd16494    1 EDDCPICYEEMLEKGE--PLTYCRFG--CGNN-VHIHCMKVWAEhqrQSDEPVTCPLC 53
 
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 ...
 5-116 1.86e-51

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: 170.89  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELIFGTVHVEGNMMVHRNCLYLSSNLIQRGEKKLSIMNFLKEDIEAEVNRCRLLKCCYCRRLGANIWCCK 84
Cdd:cd15669    1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442617064  85 SGCRRTFHTKCGVDNLAQNQFCDTYNSFCHQH 116
Cdd:cd15669   81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 30-116 9.57e-24

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: 95.09  E-value: 9.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   30 HRNCLYLSSNLIQRGEKKlsiMNFLKEDIEAEVNRCRLLKCCYCR-RLGANIWCCKSGCRRTFHTKCGVDNLAQNQFC-- 106
Cdd:pfam13771   1 HVVCALWSPELVQRGNDS---MGFPIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFDed 77

                          90
                  ....*....|.
gi 442617064  107 -DTYNSFCHQH 116
Cdd:pfam13771  78 nGTFKSYCKKH 88
RING-CH-C4HC3_ZSWM2 cd16494
RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein ...
 129-183 8.74e-04

RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3, and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination and two RING fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This model corresponds to the first RING finger, which is a C4HC3-type RING-CH finger, also known as vRING or RINGv, rather than the canonical C3H2C3-type RING-H2 finger.


Pssm-ID: 438157 [Multi-domain]  Cd Length: 57  Bit Score: 37.70  E-value: 8.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442617064 129 DEECLLCAEDVVAKGErfSVVTCLYApcCRNGwFHRRCLQRYAN---SSGYFFKCPLC 183
Cdd:cd16494    1 EDDCPICYEEMLEKGE--PLTYCRFG--CGNN-VHIHCMKVWAEhqrQSDEPVTCPLC 53
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
 131-184 7.42e-03

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 38.82  E-value: 7.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442617064 131 ECLLCAEDVVaKGERFSVVTClyapccrNGWFHRRCLQRYANssGYFFKCPLCN 184
Cdd:COG5540  325 ECAICMSNFI-KNDRLRVLPC-------DHRFHVGCVDKWLL--GYSNKCPVCR 368
 
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 ...
 5-116 1.86e-51

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: 170.89  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELIFGTVHVEGNMMVHRNCLYLSSNLIQRGEKKLSIMNFLKEDIEAEVNRCRLLKCCYCRRLGANIWCCK 84
Cdd:cd15669    1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442617064  85 SGCRRTFHTKCGVDNLAQNQFCDTYNSFCHQH 116
Cdd:cd15669   81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 30-116 9.57e-24

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: 95.09  E-value: 9.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   30 HRNCLYLSSNLIQRGEKKlsiMNFLKEDIEAEVNRCRLLKCCYCR-RLGANIWCCKSGCRRTFHTKCGVDNLAQNQFC-- 106
Cdd:pfam13771   1 HVVCALWSPELVQRGNDS---MGFPIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFDed 77

                          90
                  ....*....|.
gi 442617064  107 -DTYNSFCHQH 116
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); ...
 5-116 9.92e-13

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


Pssm-ID: 277143  Cd Length: 116  Bit Score: 64.72  E-value: 9.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELIFGTVHVEGNMMVHRNCLYLSSNLIQRG-EKKLSIMNFLKEDIEAEVNRCRLLKCCYCRRLGANIWCC 83
Cdd:cd15673    1 CGFCKSGEENKETGGKLASGEKIAAHHNCMLFSSGLVQYVsPNENDFGGFDIEDVKKEIKRGRKLKCNLCKKTGATIGCD 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 442617064  84 KSGCRRTFHTKCGVDNLAQNQFCD---TYNSFCHQH 116
Cdd:cd15673   81 VKQCKKTYHYHCAKKDDAKIIERNsqgIYRVYCKNH 116
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 5-116 5.67e-10

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: 56.89  E-value: 5.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELifGTVHVEGNMMV--HRNCLYLSSNLIQRGEKKLSIMNFLKEDIEAEVNRCRLLKCCYCRRLGANIWC 82
Cdd:cd15710    1 CGFCRSNREKEC--GQLLISENQKVaaHHKCMLFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGC 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442617064  83 CKSGCRRTFHTKCGVDNLAQ---NQFCDTYNSFCHQH 116
Cdd:cd15710   79 DVKTCHRTYHYYCALHDKAQireNPSQGIYMIYCRKH 115
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 5-116 1.35e-09

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277182 [Multi-domain]  Cd Length: 115  Bit Score: 55.67  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELIFgtVHVEGNMMVHRNCLYLSSNLIQRGEKKLSIMN--FLKEDIEAEVNRCRLLKCCYCRRLGANIWC 82
Cdd:cd15712    1 CAFCPKGEEYSIMY--FAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDrrFDVESVLNEIKRGKRLKCNFCRKKGATVGC 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442617064  83 CKSGCRRTFHTKCGVDNLA---QNQFCDTYNSFCHQH 116
Cdd:cd15712   79 EERACRRSYHYFCALCDDAaieTDEVRGIYRVFCQKH 115
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 5-116 1.03e-08

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: 53.55  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELIFGTVHVEG--NMMVHRNCLYLSSNLIQ-RGEKKLSIMNFLKEDIEAEVNRCRLLKCCYCRRLGANIW 81
Cdd:cd15711    1 CGFCHAGEEENETRGKLHIFNakKAAAHYKCMLFSSGTVQlTTTSRAEFGDFDIKTVIQEIKRGKRMKCTLCSQLGATIG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 442617064  82 CCKSGCRRTFHTKCGVDNLA---QNQFCDTYNSFCHQH 116
Cdd:cd15711   81 CEIKACVKTYHYHCGVQDKAkyiENMSRGIYKLYCKNH 118
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 5-116 7.84e-08

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: 50.66  E-value: 7.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDELIFGTV-HVEGNMMVHRNCLYLSSNLIQRGEKKLSIMNFLKEDIEAevnrcRLLKCCYCR-RLGANIWC 82
Cdd:cd15571    1 CALCPRSGGALKGGGALkTTSDGLWVHVVCALWSPEVYFDDGTLLEVEGVSKIPKRR-----KKLKCSICGkRGGACIQC 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442617064  83 CKSGCRRTFHTKCGVDN-LAQNQFCDTYN--SFCHQH 116
Cdd:cd15571   76 SYPGCPRSFHVSCAIRAgCLFEFEDGPGNfvVYCPKH 112
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 5-116 3.85e-07

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: 48.50  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLS-GERDELIFGTV-HVEGNMMVHRNCLYLSSNLIQRGEKKLsimnflkEDIEAEVNRCRLLKCCYCRRLGANIWC 82
Cdd:cd15694    1 CALCLKyGDADSKDAGRLlYIGQNEWTHVNCAIWSAEVFEENDGSL-------KNVHAAVARGRQMRCEHCQKIGATVGC 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442617064  83 CKSGCRRTFHTKCGvdNLAQNQFCDTYNSFCHQH 116
Cdd:cd15694   74 CLSACLSNFHFMCA--RASRCCFQDDKKVFCQKH 105
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 29-116 4.03e-06

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: 45.47  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064  29 VHRNCLYLSSNLIQRGEKKLsimnflkEDIEAEVNRCRLLKCCYCRRLGANIWCCKSGCRRTFHTKCGVDNLAqnQFCDT 108
Cdd:cd15664   27 VHINCALWSAEVFEEDDGSL-------QNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCARKAEC--VFQDD 97


                 ....*...
gi 442617064 109 YNSFCHQH 116
Cdd:cd15664   98 KKVFCPAH 105
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 25-116 1.69e-05

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: 43.46  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064  25 GNMMVHRNCLYLSSNLIQrgekklsIMNFLKEDIEAEVNRCRLLKCCYCRRLGANIWCCKSGCRRTFHTKCGVdnlAQNQ 104
Cdd:cd15665    7 GEVYAHHCCAAWSEGVCQ-------TEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAA---AAGC 76

                         90
                 ....*....|....
gi 442617064 105 FCD--TYNSFCHQH 116
Cdd:cd15665   77 FQDikTLTLFCPEH 90
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 5-116 2.57e-05

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: 43.06  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLSGERDEL---IFGTVHvegNMMVHRNCLYLSSNLIQRGEKklsiMNFLKEDIEAevnrCRLLKCCYCRRLGANIW 81
Cdd:cd15668    1 CVFCKRGPHYKGlgdLFGPYY---EVWVHEDCAVWAPGVYLVGGK----LYGLEEAVWV----AKQSVCSSCQQTGATIG 69

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 442617064  82 CCKSGCRRTFHTKCGVDNLAQNQfCDTYNSFCHQH 116
Cdd:cd15668   70 CLHKGCKAKYHYPCAVESGCQLD-EENFSLLCPKH 103
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 5-116 2.92e-04

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: 40.37  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLCLS-GERDELIFGTV-HVEGNMMVHRNCLYLSSNLIQRGEKKLsimnflkEDIEAEVNRCRLLKCCYCRRLGANIWC 82
Cdd:cd15693    3 CALCLKyGDDSANDAGRLlYIGQNEWTHVNCALWSAEVFEDDDGSL-------KNVHMAVIRGKQLRCEFCQKPGATVGC 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 442617064  83 CKSGCRRTFHTKCGvdNLAQNQFCDTYNSFCHQH 116
Cdd:cd15693   76 CLTSCTSNYHFMCS--RAKNCVFLEDKKVYCQRH 107
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
57-116 5.25e-04

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 39.63  E-value: 5.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442617064   57 DIEAEVNRCRLLKCCYCR-RLGANIWCCKSGCRRTFHTKC----GVDNLAQNQFCDTYNSFCHQH 116
Cdd:pfam13832  45 DVSRIPPERWKLKCVFCKkRSGACIQCSKGRCTTAFHVTCaqaaGVYMEPEDWPNVVVIAYCQKH 109
RING-CH-C4HC3_ZSWM2 cd16494
RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein ...
 129-183 8.74e-04

RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3, and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination and two RING fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This model corresponds to the first RING finger, which is a C4HC3-type RING-CH finger, also known as vRING or RINGv, rather than the canonical C3H2C3-type RING-H2 finger.


Pssm-ID: 438157 [Multi-domain]  Cd Length: 57  Bit Score: 37.70  E-value: 8.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442617064 129 DEECLLCAEDVVAKGErfSVVTCLYApcCRNGwFHRRCLQRYAN---SSGYFFKCPLC 183
Cdd:cd16494    1 EDDCPICYEEMLEKGE--PLTYCRFG--CGNN-VHIHCMKVWAEhqrQSDEPVTCPLC 53
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 69-95 2.66e-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: 37.23  E-value: 2.66e-03
                         10        20
                 ....*....|....*....|....*..
gi 442617064  69 KCCYCRRLGANIWCCKSGCRRTFHTKC 95
Cdd:cd15696   44 RCAFCKHLGATIKCCEEKCTQMYHYPC 70
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 5-95 3.18e-03

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: 37.28  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617064   5 CVLClSGERDELIFGTV---HVEGNMMVHRNCLYLSSNLI--QRGekklSIMNflkedIEAEVNRCRLLKCCYCRRLGAN 79
Cdd:cd15666    1 CVLC-GGEGDGDTDGPGrllNLDVDKWVHLNCALWSYEVYetQNG----ALMN-----VEEALRRALTTTCSHCGRTGAT 70

                         90
                 ....*....|....*.
gi 442617064  80 IWCCKSGCRRTFHTKC 95
Cdd:cd15666   71 VPCFKPRCANVYHLPC 86
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 68-116 3.65e-03

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: 37.42  E-value: 3.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442617064  68 LKCCYCR-RLGANIWCCKSGCRRTFHTKCGVD-NLAQNQFCDTYN------SFCHQH 116
Cdd:cd15671   56 LVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQhGLEMKTILEDEDdevkfkSYCPKH 112
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
 131-184 7.42e-03

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 38.82  E-value: 7.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442617064 131 ECLLCAEDVVaKGERFSVVTClyapccrNGWFHRRCLQRYANssGYFFKCPLCN 184
Cdd:COG5540  325 ECAICMSNFI-KNDRLRVLPC-------DHRFHVGCVDKWLL--GYSNKCPVCR 368
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 68-98 8.32e-03

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: 36.01  E-value: 8.32e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 442617064  68 LKCCYCRRLGANIWCCKSGCRRTFHTKCGVD 98
Cdd:cd15700   57 AKCSSCQGAGATVGCCHKGCTQSYHYICAVE 87
 
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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