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. .

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042  16 CAFCRTNRDKECGQLLVSDSQKVAAHHKCMLFSSALVTSHSDSENIGGFSIEDVKKEIKRGNKLMCSSCHRPGATIGCDV 95
Cdd:cd15710     1 CGFCRSNREKECGQLLISENQKVAAHHKCMLFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2059434042  96 KTCRRTYHYYCAVKDKAQIKENPSQGIYLVYCRKH 130
Cdd:cd15710    81 KTCHRTYHYYCALHDKAQIRENPSQGIYMIYCRKH 115

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. .

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042  16 CAFCRTNRDKECGQLLVSDSQKVAAHHKCMLFSSALVTSHSDSENIGGFSIEDVKKEIKRGNKLMCSSCHRPGATIGCDV 95
Cdd:cd15710     1 CGFCRSNREKECGQLLISENQKVAAHHKCMLFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2059434042  96 KTCRRTYHYYCAVKDKAQIKENPSQGIYLVYCRKH 130
Cdd:cd15710    81 KTCHRTYHYYCALHDKAQIRENPSQGIYMIYCRKH 115

hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine phosphoribosyltransferase. Sequence differences as small as a single residue can affect whether members of this family act on hypoxanthine and guanine or hypoxanthine only. The designation of this model as equivalog reflects hypoxanthine specificity and does not reflect whether or not guanine can replace hypoxanthine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 452 VYIPHGLILDRTERLAREIMKEMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTND-----------QSTGE 520
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIA---------VPVQVDfmavssygngmQSSGD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 521 IKVIGGDDLSTLtGKNVLIVEDIIDTGKTMKTLLQLLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGYAL 600
Cdd:TIGR01203  72 VKILKDLDLDIK-GKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGL 150

                         170
                  ....*....|
gi 2059434042 601 DYNEYFRDLN 610
Cdd:TIGR01203 151 DYAERYRNLP 160

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042  41 HHKCMLFSSALVTSHSDSeniGGFSIEDVKKEIKRGNKLMCSSCHRP-GATIGCDVKTCRRTYHYYCAVKDKAQIKENPS 119
Cdd:pfam13771   1 HVVCALWSPELVQRGNDS---MGFPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDED 77

                          90
                  ....*....|.
gi 2059434042 120 QGIYLVYCRKH 130
Cdd:pfam13771  78 NGTFKSYCKKH 88

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 456 HGLILDRTERLAREIMKEMGGHHIVALCVLKGGYKFFADL-------LDYIKALNRNSDRSIPMTNDQSTGEIKviggdd 528
Cdd:pfam00156   8 NPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILarrldvpLAFVRKVSYNPDTSEVMKTSSALPDLK------ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2059434042 529 lstltGKNVLIVEDIIDTGKTMKTLLQLLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEvPDKFVVGYALDYN 603
Cdd:pfam00156  82 -----GKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDER 150

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2059434042   80 MCSSCHRP---GATIGCDvkTCRRTYHYYCavkdkAQIKENPSQGIYLVYCRKH 130
Cdd:smart00249   1 YCSVCGKPddgGELLQCD--GCDRWYHQTC-----LGPPLLEEEPDGKWYCPKC 47

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. .

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042  16 CAFCRTNRDKECGQLLVSDSQKVAAHHKCMLFSSALVTSHSDSENIGGFSIEDVKKEIKRGNKLMCSSCHRPGATIGCDV 95
Cdd:cd15710     1 CGFCRSNREKECGQLLISENQKVAAHHKCMLFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2059434042  96 KTCRRTYHYYCAVKDKAQIKENPSQGIYLVYCRKH 130
Cdd:cd15710    81 KTCHRTYHYYCALHDKAQIRENPSQGIYMIYCRKH 115

hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine phosphoribosyltransferase. Sequence differences as small as a single residue can affect whether members of this family act on hypoxanthine and guanine or hypoxanthine only. The designation of this model as equivalog reflects hypoxanthine specificity and does not reflect whether or not guanine can replace hypoxanthine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 452 VYIPHGLILDRTERLAREIMKEMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTND-----------QSTGE 520
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIA---------VPVQVDfmavssygngmQSSGD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 521 IKVIGGDDLSTLtGKNVLIVEDIIDTGKTMKTLLQLLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGYAL 600
Cdd:TIGR01203  72 VKILKDLDLDIK-GKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGL 150

                         170
                  ....*....|
gi 2059434042 601 DYNEYFRDLN 610
Cdd:TIGR01203 151 DYAERYRNLP 160

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFCHAGDEENETRGMLHtdNSKKVAAHYKCMLFSSGTVQLTTTSRAEFGNFDVKTVIQEIKRGKRMKCTLCTQLGATIG 295
Cdd:cd15673     1 CGFCKSGEENKETGGKLA--SGEKIAAHHNCMLFSSGLVQYVSPNENDFGGFDIEDVKKEIKRGRKLKCNLCKKTGATIG 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2059434042 296 CEIKACVKTYHYHCGLQDKAKYIENMARGIYKLYCKNH 333
Cdd:cd15673    79 CDVKQCKKTYHYHCAKKDDAKIIERNSQGIYRVYCKNH 116

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042  16 CAFCrtNRDKECGQLLVSDSQKVAAHHKCMLFSSALVTSHS-DSENIG-GFSIEDVKKEIKRGNKLMCSSCHRPGATIGC 93
Cdd:cd15712     1 CAFC--PKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEyNPLNLDrRFDVESVLNEIKRGKRLKCNFCRKKGATVGC 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2059434042  94 DVKTCRRTYHYYCAVKDKAQIKENPSQGIYLVYCRKH 130
Cdd:cd15712    79 EERACRRSYHYFCALCDDAAIETDEVRGIYRVFCQKH 115

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. .

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFCHAgDEENETrGMLHTDNSKKVAAHYKCMLFSSGTVQLTTTSRAeFGNFDVKTVIQEIKRGKRMKCTLCTQLGATIG 295
Cdd:cd15710     1 CGFCRS-NREKEC-GQLLISENQKVAAHHKCMLFSSALVSSHSDSEN-LGGFSIEDVQKEIKRGTKLMCSLCHCPGATIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2059434042 296 CEIKACVKTYHYHCGLQDKAKYIENMARGIYKLYCKNH 333
Cdd:cd15710    78 CDVKTCHRTYHYYCALHDKAQIRENPSQGIYMIYCRKH 115

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042  16 CAFCRTNRDKE--CGQLLVSDsqKVAAHHKCMLFSSALVTSHSDSENIGGFSIEDVKKEIKRGNKLMCSSCHRPGATIGC 93
Cdd:cd15669     1 CVLCGRSDDDPdkYGEKLQKD--GICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2059434042  94 DVKTCRRTYHYYCAVKDKAQikenpSQ--GIYLVYCRKH 130
Cdd:cd15669    79 AVKGCRRSFHFPCGLENGCV-----TQffGEYRSFCWEH 112

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFCHAGDEENetrgMLHTDNSKKVAAHYKCMLFSSGTVQLTTTSRAEFG-NFDVKTVIQEIKRGKRMKCTLCTQLGATI 294
Cdd:cd15712     1 CAFCPKGEEYS----IMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDrRFDVESVLNEIKRGKRLKCNFCRKKGATV 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2059434042 295 GCEIKACVKTYHYHCGLQDKAKYIENMARGIYKLYCKNH 333
Cdd:cd15712    77 GCEERACRRSYHYFCALCDDAAIETDEVRGIYRVFCQKH 115

hypoxanthine-guanine phosphoribosyltransferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 464 ERLAREIMKEMGGHHIVALCVLKGGYKFFADLL---------DYIKALNRNsdrsipmtNDQSTGEI--KVIGGDDLStl 532
Cdd:PRK09162   27 DRMADEITADLADENPLVLCVMGGGLVFTGQLLprldfplefDYLHATRYR--------NETTGGELvwKVKPRESLK-- 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059434042 533 tGKNVLIVEDIIDTGKTMKTLLQLLKQYNPKMVKVASLLVKRTPRSV-GYRPDFVGFEVPDKFVVGYALDYNEYFRDL 609
Cdd:PRK09162   97 -GRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYWRNL 173

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFC-HAGDEENETRGMLHTDNSKKVaaHYKCMLFSSGTVQLTTTSRaefgnfDVKTVIQEIKRGKRMKCTLCTQ-LGAT 293
Cdd:cd15571     1 CALCpRSGGALKGGGALKTTSDGLWV--HVVCALWSPEVYFDDGTLL------EVEGVSKIPKRRKKLKCSICGKrGGAC 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2059434042 294 IGCEIKACVKTYHYHCGLQDKAKYIENMARGIYKLYCKNH 333
Cdd:cd15571    73 IQCSYPGCPRSFHVSCAIRAGCLFEFEDGPGNFVVYCPKH 112

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFCHAGDEENETRGMLHTDNskKVAAHYKCMLFSSGTVQlTTTSRAEFGNFDVKTVIQEIKRGKRMKCTLCTQLGATIG 295
Cdd:cd15669     1 CVLCGRSDDDPDKYGEKLQKD--GICAHYFCLLFSSGLPQ-RGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2059434042 296 CEIKACVKTYHYHCGLQDKAKyieNMARGIYKLYCKNH 333
Cdd:cd15669    78 CAVKGCRRSFHFPCGLENGCV---TQFFGEYRSFCWEH 112

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 456 HGLILDRTERLAREIMKEMGGHHIVALCVLKGGYKFFADL-------LDYIKALNRNSDRSIPMTNDQSTGEIKviggdd 528
Cdd:pfam00156   8 NPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILarrldvpLAFVRKVSYNPDTSEVMKTSSALPDLK------ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2059434042 529 lstltGKNVLIVEDIIDTGKTMKTLLQLLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEvPDKFVVGYALDYN 603
Cdd:pfam00156  82 -----GKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDER 150

hypoxanthine-guanine phosphoribosyltransferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 482 LCVLKGGYKFFADLLDYIkalnrnSDRSIPM-----------TNDQSTGEIKVIGgDDLSTLTGKNVLIVEDIIDTGKTM 550
Cdd:PTZ00271   62 LCVLKGSFIFTADLARFL------ADEGVPVkveficassygTGVETSGQVRMLL-DVRDSVENRHILIVEDIVDSAITL 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2059434042 551 KTLLQLLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGYALDYNEYFRDL 609
Cdd:PTZ00271  135 QYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDYAESYREL 193

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042  16 CAFCRTNRD---KECGQLLVSdSQKVAAHHKCMLFSSALVtshsdsENIGGfSIEDVKKEIKRGNKLMCSSCHRPGATIG 92
Cdd:cd15664     1 CALCGVYGDdepNDAGRLLYC-GQDEWVHINCALWSAEVF------EEDDG-SLQNVHSAVSRGRMMKCELCGKPGATVG 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2059434042  93 CDVKTCRRTYHYYCAVKDKAQIKENPSqgiylVYCRKH 130
Cdd:cd15664    73 CCLKSCPANYHFMCARKAECVFQDDKK-----VFCPAH 105

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFC-HAGDEE-NETRGMLHTDNSKKVaaHYKCMLFSsgtvqltttsrAE-FGNFD--VKTVIQEIKRGKRMKCTLCTQL 290
Cdd:cd15664     1 CALCgVYGDDEpNDAGRLLYCGQDEWV--HINCALWS-----------AEvFEEDDgsLQNVHSAVSRGRMMKCELCGKP 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2059434042 291 GATIGCEIKACVKTYHYHCGLQDKAKYIENMargiyKLYCKNH 333
Cdd:cd15664    68 GATVGCCLKSCPANYHFMCARKAECVFQDDK-----KVFCPAH 105

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 214 QRCGFC--HAGDEENETRGMLHTDNSKkvAAHYKCMLFSSGTVQLTTTSraefgnfdVKTVIQEIKRGKRMKCTLCTQLG 291
Cdd:cd15693     1 RQCALClkYGDDSANDAGRLLYIGQNE--WTHVNCALWSAEVFEDDDGS--------LKNVHMAVIRGKQLRCEFCQKPG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2059434042 292 ATIGCEIKACVKTYHYHCGLQDKAKYIENMargiyKLYCKNH 333
Cdd:cd15693    71 ATVGCCLTSCTSNYHFMCSRAKNCVFLEDK-----KVYCQRH 107

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFCHA-GDEENETRG-MLHTDNSKKVaaHYKCMLFSSGTVQlttTSRAEFGNFDvktviQEIKRGKRMKCTLCTQLGAT 293
Cdd:cd15666     1 CVLCGGeGDGDTDGPGrLLNLDVDKWV--HLNCALWSYEVYE---TQNGALMNVE-----EALRRALTTTCSHCGRTGAT 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2059434042 294 IGCEIKACVKTYHYHCGLQDKAKYIENmaRGIyklYCKNH 333
Cdd:cd15666    71 VPCFKPRCANVYHLPCAIKDGCMFFKD--KTM---LCPSH 105

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2059434042  69 VKKEIKRGNKLMCSSCHRPGATIGCDVKTCRRTYHYYCAVKDKAQIKENPsqgiYLVYCRKH 130
Cdd:cd15700    47 LQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEEN----FSLRCPKH 104

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 242 AHYKCMLFSSGTVQLTTtsrAEFGNFDvKTVIQEIKRgkrmKCTLCTQLGATIGCEIKACVKTYHYHC-----GLQDkak 316
Cdd:cd15665    11 AHHCCAAWSEGVCQTED---GALENVD-KAVAKALSQ----KCSFCLRYGASISCRMPSCSKSFHFPCaaaagCFQD--- 79

                          90
                  ....*....|....*..
gi 2059434042 317 yIENMArgiykLYCKNH 333
Cdd:cd15665    80 -IKTLT-----LFCPEH 90

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059434042 216 CGFCHA---GDEENETRgMLHTDnsKKVAAHYKCMLFSSgtvQLTTTSRAEFGNFDVKtviqeIKRGKRMKCTLCTQLGA 292
Cdd:cd15697     1 CCFCHEegdGLTDGPAR-LLNLD--LDLWVHLNCALWST---EVYETQAGALINVELA-----LRRGLQMKCVFCHKTGA 69