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Conserved domains on  [gi|2462511422|ref|XP_054193654|]
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histone-lysine N-methyltransferase ASH1L isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 421-561 4.72e-102

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


:

Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 319.24  E-value: 4.72e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  421 CLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSC 500
Cdd:cd19174      1 GLERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSC 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  501 DPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCRGIIGG 561
Cdd:cd19174     81 DPNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIGG 141
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 718-823 4.26e-58

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


:

Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 194.92  E-value: 4.26e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  718 ARLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNA 797
Cdd:cd05525      1 ARLAQVLKEICDAIITYKDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNA 80

                           90       100
                   ....*....|....*....|....*.
gi 2462511422  798 EKYYGRKSPVGRDVCRLRKAYYNARH 823
Cdd:cd05525     81 EKYYGRKSPIGRDVCRLRKAYYQAKH 106
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 940-1074 4.93e-54

BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


:

Pssm-ID: 240068  Cd Length: 121  Bit Score: 183.94  E-value: 4.93e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  940 QGDCVYLMRDSRRTpdghpvrqsyrllshinrdKLDIFRIEKLWKNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFRV 1019
Cdd:cd04717      6 VGDCVYVANPEDPS-------------------KPIIFRIERLWKDEDGEKFFFGCWFYRPEETFHEPTRKFYKNEVFKS 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422 1020 PLYEIIPLEAVVGTCCVLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKIHR 1074
Cdd:cd04717     67 PLYETVPVEEIVGKCAVMDVKDYIKGRPTEISEEDVYVCESRYNESAKSFKKIKT 121
PHD_ASH1L cd15548
PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like ...
 861-903 1.29e-26

PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like protein, or absent small and homeotic disks protein 1 homolog, or lysine N-methyltransferase 2H, is a protein belonging to the Trithorax family. It methylates Lys36 of histone H3 independently of transcriptional elongation to promote the establishment of Hox gene expression by counteracting Polycomb silencing. It can suppress interleukin-6 (IL-6), and tumor necrosis factor (TNF) production in Toll-like receptor (TLR)-triggered macrophages, and inflammatory autoimmune diseases by inducing the ubiquitin-editing enzyme A20. ASH1L contains an associated with SET domain (AWS), a SET domain, a post-SET domain, a bromodomain, a bromo-adjacent homology domain (BAH), and a plant homeodomain (PHD) finger.


:

Pssm-ID: 277023  Cd Length: 43  Bit Score: 102.93  E-value: 1.29e-26
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462511422  861 IRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQC 903
Cdd:cd15548      1 IRCICGLYKDEGLMIQCEKCMVWQHCDCMGVNDDVEHYLCEQC 43
AWS smart00570
associated with SET domains; subdomain of PRESET
 367-418 1.03e-17

associated with SET domains; subdomain of PRESET


:

Pssm-ID: 197795  Cd Length: 50  Bit Score: 77.83  E-value: 1.03e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2462511422   367 EATTCNCKKPDDDtRKGCVDDCLNRMIFAECsPNTCPCGEQCCNQRIQRHEW 418
Cdd:smart00570    1 DIMTCECKPTDDD-ETACGSDCLNRMLFIEC-SSSCPCGSYCSNQRFQKRQY 50
 
Name Accession Description Interval E-value
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 421-561 4.72e-102

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 319.24  E-value: 4.72e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  421 CLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSC 500
Cdd:cd19174      1 GLERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSC 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  501 DPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCRGIIGG 561
Cdd:cd19174     81 DPNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIGG 141
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 718-823 4.26e-58

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 194.92  E-value: 4.26e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  718 ARLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNA 797
Cdd:cd05525      1 ARLAQVLKEICDAIITYKDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNA 80

                           90       100
                   ....*....|....*....|....*.
gi 2462511422  798 EKYYGRKSPVGRDVCRLRKAYYNARH 823
Cdd:cd05525     81 EKYYGRKSPIGRDVCRLRKAYYQAKH 106
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 940-1074 4.93e-54

BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240068  Cd Length: 121  Bit Score: 183.94  E-value: 4.93e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  940 QGDCVYLMRDSRRTpdghpvrqsyrllshinrdKLDIFRIEKLWKNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFRV 1019
Cdd:cd04717      6 VGDCVYVANPEDPS-------------------KPIIFRIERLWKDEDGEKFFFGCWFYRPEETFHEPTRKFYKNEVFKS 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422 1020 PLYEIIPLEAVVGTCCVLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKIHR 1074
Cdd:cd04717     67 PLYETVPVEEIVGKCAVMDVKDYIKGRPTEISEEDVYVCESRYNESAKSFKKIKT 121
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 421-541 1.22e-42

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 151.72  E-value: 1.22e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422   421 CLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMiEQYHNHS--DHYCLNLDSGMVIDSYRMGNEARFINH 498
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERP-KAYDTDGakAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2462511422   499 SCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFN 541
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
426-557 8.33e-32

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 121.22  E-value: 8.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  426 RAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHsdHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCE 505
Cdd:COG2940     12 PSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLH--TYLFELDDDGVIDGALGGNPARFINHSCDPNCE 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462511422  506 MqkWSVNGvyRIGLYALKDMPAGTELTYDYNFhsFNVEKQQLCKCGfeKCRG 557
Cdd:COG2940     90 A--DEEDG--RIFIVALRDIAAGEELTYDYGL--DYDEEEYPCRCP--NCRG 133
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 431-536 4.28e-30

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 115.31  E-value: 4.28e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGE-VVSEQEFRNRMIEQYHNHSDH------YCLNLDSGMVID--SYRMGNEARFINHSCD 501
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRlwgpylFTLDEDSEYCIDarALYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462511422  502 PNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYN 536
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
PHD_ASH1L cd15548
PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like ...
 861-903 1.29e-26

PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like protein, or absent small and homeotic disks protein 1 homolog, or lysine N-methyltransferase 2H, is a protein belonging to the Trithorax family. It methylates Lys36 of histone H3 independently of transcriptional elongation to promote the establishment of Hox gene expression by counteracting Polycomb silencing. It can suppress interleukin-6 (IL-6), and tumor necrosis factor (TNF) production in Toll-like receptor (TLR)-triggered macrophages, and inflammatory autoimmune diseases by inducing the ubiquitin-editing enzyme A20. ASH1L contains an associated with SET domain (AWS), a SET domain, a post-SET domain, a bromodomain, a bromo-adjacent homology domain (BAH), and a plant homeodomain (PHD) finger.


Pssm-ID: 277023  Cd Length: 43  Bit Score: 102.93  E-value: 1.29e-26
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462511422  861 IRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQC 903
Cdd:cd15548      1 IRCICGLYKDEGLMIQCEKCMVWQHCDCMGVNDDVEHYLCEQC 43
BROMO smart00297
bromo domain;
719-816 7.16e-20

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 85.79  E-value: 7.16e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422   719 RLAQIFKEICDGIISYKDSSRqaLAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAE 798
Cdd:smart00297    3 KLQKKLQELLKAVLDKLDSHP--LSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNAR 80

                            90
                    ....*....|....*...
gi 2462511422   799 KYYGRKSPVGRDVCRLRK 816
Cdd:smart00297   81 TYNGPDSEVYKDAKKLEK 98
BAH smart00439
Bromo adjacent homology domain;
941-1072 3.50e-19

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 84.65  E-value: 3.50e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422   941 GDCVYLMRDSRRTPdghpvrqsyrllshinrdkLDIFRIEKLW--KNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFR 1018
Cdd:smart00439    5 GDFVLVEPDDADEP-------------------YYIGRIEEIFetKKNSESKMVRVRWFYRPEETVLEKAALFDKNEVFL 65

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422  1019 VPLYEIIPLEAVVGTCCVLDLYTYCKGRPKGV-KEQDVYICDYRLDKSAHLFYKI 1072
Cdd:smart00439   66 SDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSiGEPDVFFCESAYDPEKGSFKKL 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 941-1072 7.84e-19

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 83.51  E-value: 7.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  941 GDCVYLmrdsrrtpDGHPVRQSYRllshinrdkldIFRIEKLWKNEKEERF-AFGHHYFRPHETHHSPSRRFYHNELFRV 1019
Cdd:pfam01426    6 GDFVLV--------EPDDADEPYY-----------VARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLS 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462511422 1020 PLYEIIPLEAVVGTCCVLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKI 1072
Cdd:pfam01426   67 DEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKEPDDFFCELLYDPKTKSFKKL 119
AWS smart00570
associated with SET domains; subdomain of PRESET
 367-418 1.03e-17

associated with SET domains; subdomain of PRESET


Pssm-ID: 197795  Cd Length: 50  Bit Score: 77.83  E-value: 1.03e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2462511422   367 EATTCNCKKPDDDtRKGCVDDCLNRMIFAECsPNTCPCGEQCCNQRIQRHEW 418
Cdd:smart00570    1 DIMTCECKPTDDD-ETACGSDCLNRMLFIEC-SSSCPCGSYCSNQRFQKRQY 50
AWS pfam17907
AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...
 378-416 3.06e-17

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc binding domain. The full AWS domain contains 8 cysteines. This entry represents the N-terminal part of the domain, with the C-terminal part interwoven with the SET domain.


Pssm-ID: 465559  Cd Length: 39  Bit Score: 76.31  E-value: 3.06e-17
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462511422  378 DDTRKGCVDDCLNRMIFAECSPNTCPCGEQCCNQRIQRH 416
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 728-813 2.48e-13

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 66.57  E-value: 2.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  728 CDGIISYKDssRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPV 807
Cdd:pfam00439    1 CLEILDKLM--EHPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVI 78


                   ....*.
gi 2462511422  808 GRDVCR 813
Cdd:pfam00439   79 YKAAEK 84
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 719-810 6.75e-09

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 59.43  E-value: 6.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  719 RLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAE 798
Cdd:COG5076    142 LLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCK 221

                           90
                   ....*....|..
gi 2462511422  799 KYYGRKSPVGRD 810
Cdd:COG5076    222 LYNGPDSSVYVD 233
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 863-906 4.33e-07

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 47.87  E-value: 4.33e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462511422  863 CICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVE-----HYLCEQCDPR 906
Cdd:pfam00628    3 AVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAeipsgEWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 863-903 6.89e-07

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 47.21  E-value: 6.89e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 2462511422   863 CICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDV----EHYLCEQC 903
Cdd:smart00249    3 SVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeepdGKWYCPKC 47
 
Name Accession Description Interval E-value
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 421-561 4.72e-102

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 319.24  E-value: 4.72e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  421 CLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSC 500
Cdd:cd19174      1 GLERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSC 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  501 DPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCRGIIGG 561
Cdd:cd19174     81 DPNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIGG 141
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 421-556 3.36e-68

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins; This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins.


Pssm-ID: 380929  Cd Length: 136  Bit Score: 225.21  E-value: 3.36e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  421 CLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQY-HNHSDHYCLNLDSGMVIDSYRMGNEARFINHS 499
Cdd:cd10531      1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEeLGKSNFYILSLSDDVVIDATRKGNLSRFINHS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462511422  500 CDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNvEKQQLCKCGFEKCR 556
Cdd:cd10531     81 CEPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNYN-EAKQVCLCGAQNCR 136
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 422-560 1.19e-60

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins; SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy.


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 203.97  E-value: 1.19e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  422 LERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMiEQYH--NHSDHYCLNLDSGMVIDSYRMGNEARFINHS 499
Cdd:cd19172      4 VEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRM-KEYAreGNRHYYFMALKSDEIIDATKKGNLSRFINHS 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  500 CDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQlCKCGFEKCRGIIG 560
Cdd:cd19172     83 CEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFERYGKEAQK-CYCGSPNCRGYIG 142
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 718-823 4.26e-58

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 194.92  E-value: 4.26e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  718 ARLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNA 797
Cdd:cd05525      1 ARLAQVLKEICDAIITYKDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNA 80

                           90       100
                   ....*....|....*....|....*.
gi 2462511422  798 EKYYGRKSPVGRDVCRLRKAYYNARH 823
Cdd:cd05525     81 EKYYGRKSPIGRDVCRLRKAYYQAKH 106
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 422-560 5.06e-55

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


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 187.91  E-value: 5.06e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  422 LERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmIEQYH--NHSDHYCLNLDSGMVIDSYRMGNEARFINHS 499
Cdd:cd19173      4 TEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRR-LKKAHenNITNFYMLTLDKDRIIDAGPKGNLSRFMNHS 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  500 CDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQlCKCGFEKCRGIIG 560
Cdd:cd19173     83 CQPNCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNEKKV-CRCGAPNCSGFLG 142
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 940-1074 4.93e-54

BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240068  Cd Length: 121  Bit Score: 183.94  E-value: 4.93e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  940 QGDCVYLMRDSRRTpdghpvrqsyrllshinrdKLDIFRIEKLWKNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFRV 1019
Cdd:cd04717      6 VGDCVYVANPEDPS-------------------KPIIFRIERLWKDEDGEKFFFGCWFYRPEETFHEPTRKFYKNEVFKS 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422 1020 PLYEIIPLEAVVGTCCVLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKIHR 1074
Cdd:cd04717     67 PLYETVPVEEIVGKCAVMDVKDYIKGRPTEISEEDVYVCESRYNESAKSFKKIKT 121
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 422-560 1.41e-45

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins; This family includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3, also termed protein SET DOMAIN GROUP 4 or protein stamen loss), ASH1 homolog 3 (ASHH3, also termed protein SET DOMAIN GROUP 7) and homolog 4 (ASHH4, also termed protein SET DOMAIN GROUP 24). They all function as histone-lysine N-methyltransferases (EC 2.1.1.43).


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 160.66  E-value: 1.41e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  422 LERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHN-HSDHYCLNLDSGMVIDSYRMGNEARFINHSC 500
Cdd:cd19175      2 MKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKgEKNFYMCEIDKDMVIDATFKGNLSRFINHSC 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  501 DPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQqlCKCGFEKCRGIIG 560
Cdd:cd19175     82 DPNCELQKWQVDGETRIGVFAIRDIKKGEELTYDYQFVQFGADQD--CHCGSKNCRGKLG 139
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 422-560 1.01e-44

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation.


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 158.17  E-value: 1.01e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  422 LERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRM-IEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSC 500
Cdd:cd19210      4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIrYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCC 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  501 DPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKqQLCKCGFEKCRGIIG 560
Cdd:cd19210     84 QPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNGK-TVCKCGAPNCSGFLG 142
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 423-560 2.09e-43

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 3 (NSD3) and similar proteins; NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. NSD3 is amplified and overexpressed in multiple cancer types, including acute myeloid leukemia (AML), breast, lung, pancreatic and bladder cancers, as well as squamous cell carcinoma of the head and neck (SCCHN). NSD3 contributes to tumorigenesis by interacting with bromodomain-containing protein 4 (BRD4), the bromodomain and extraterminal (BET) protein, which is a potential therapeutic target in acute myeloid leukemia (AML). NSD3 is amplified in primary tumors and cell lines from breast carcinoma, and can promote the cell viability of small-cell lung cancer and pancreatic ductal adenocarcinoma. High NSD3 expression is implicated in poor grade and heavy smoking history in SCCHN. Thus, NSD3 may serve as a potential druggable target for selective cancer therapy.


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 154.70  E-value: 2.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  423 ERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNH-SDHYCLNLDSGMVIDSYRMGNEARFINHSCD 501
Cdd:cd19212      5 EIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSvTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCN 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462511422  502 PNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQlCKCGFEKCRGIIG 560
Cdd:cd19212     85 PNCETQKWTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTE-CHCGADNCSGFLG 142
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 421-541 1.22e-42

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 151.72  E-value: 1.22e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422   421 CLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMiEQYHNHS--DHYCLNLDSGMVIDSYRMGNEARFINH 498
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERP-KAYDTDGakAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2462511422   499 SCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFN 541
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYAN 123
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 426-560 5.43e-42

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-36' (H3K36me) methyltransferase activity. NSD2 has been shown to mediate di- and trimethylation of H3K36 and dimethylation of H4K20 in different systems, and has been characterized as a transcriptional repressor interacting with histone deacetylase HDAC1 and histone demethylase LSD1. NSD2 mediates constitutive NF-kappaB signaling for cancer cell proliferation, survival and tumor growth. It is highly overexpressed in several types of human cancers, including small-cell lung cancers, neuroblastoma, carcinomas of stomach and colon, and bladder cancers, and its overexpression tends to be associated with tumor aggressiveness. WHSC1 is frequently deleted in Wolf-Hirschhorn syndrome (WHS).


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 150.53  E-value: 5.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  426 RAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDH-YCLNLDSGMVIDSYRMGNEARFINHSCDPNC 504
Cdd:cd19211      8 KTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDITHfYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNC 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462511422  505 EMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKqQLCKCGFEKCRGIIG 560
Cdd:cd19211     88 ETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEK-TVCRCGAPNCSGFLG 142
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 367-557 1.93e-37

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins; SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining.


Pssm-ID: 380942 [Multi-domain]  Cd Length: 254  Bit Score: 141.67  E-value: 1.93e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  367 EATTCNCKKP-----DDDTRKGCVDDCLNRMIFaECSPNtCPCGEQCCNQRIQRHewVQ-CLERFRAEEKGWGIRTKEPL 440
Cdd:cd10544     35 EPETCSCLRKygpnyDDDGCLLDFDGKYSGPVF-ECNSM-CKCSESCQNRVVQNG--LQfKLQVFKTPKKGWGLRTLEFI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  441 KAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDH-YCLN--LDSGMV----IDSYRMGNEARFINHSCDPNCEMQKWSVNG 513
Cdd:cd10544    111 PKGRFVCEYAGEVIGFEEARRRTKSQTKGDMNYiIVLRehLSSGKVletfVDPTYIGNIGRFLNHSCEPNLFMVPVRVDS 190

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462511422  514 -VYRIGLYALKDMPAGTELTYDYNFHSFNVEKQ------------QLCKCGFEKCRG 557
Cdd:cd10544    191 mVPKLALFAARDIVAGEELSFDYSGEFSNSVESvtlarqdesksrKPCLCGAENCRG 247
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 355-559 2.16e-37

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homologs, SUV39H1, SUV39H2 and similar proteins; This family includes SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. Also included are Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (SUV39H homolog) and Neurospora crassa DIM-5, both of which also methylate 'Lys-9' of histone H3.


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 141.28  E-value: 2.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  355 NVYVDVKPLSGyeattCNCKKPDDDTRKGCvddCLNRM--IFA----------------ECSPNtCPCGEQCCNQRIQRH 416
Cdd:cd10542     14 GVKIPEDFLVG-----CECTEDCHNNNPTC---CPAESgvKFAydkqgrlrlppgtpiyECNSR-CKCGPDCPNRVVQRG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  417 EWVQcLERFR-AEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEqYHNHSDHYCLNLD-----SGMVIDSYRMG 490
Cdd:cd10542     85 RKVP-LCIFRtSNGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKI-YDANGRTYLFDLDyndddCEYTVDAAYYG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  491 NEARFINHSCDPNceMQKWSVNG------VYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQ----------LCKCGFEK 554
Cdd:cd10542    163 NISHFINHSCDPN--LAVYAVWInhldprLPRIAFFAKRDIKAGEELTFDYLMTGTGGSSEStipkpkdvrvPCLCGSKN 240


                   ....*
gi 2462511422  555 CRGII 559
Cdd:cd10542    241 CRKYL 245
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 431-535 3.15e-34

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380917  Cd Length: 117  Bit Score: 127.36  E-value: 3.15e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGEVVSEQEfRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWS 510
Cdd:cd10519     12 GWGLFLKEPIKKDEFIGEYTGELISQDE-ADRRGKIYDKYNSSYLFNLNDQFVVDATRKGNKIRFANHSSNPNCYAKVMM 90

                           90       100
                   ....*....|....*....|....*
gi 2462511422  511 VNGVYRIGLYALKDMPAGTELTYDY 535
Cdd:cd10519     91 VNGDHRIGIFAKRDIEAGEELFFDY 115
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 370-536 1.50e-33

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380936 [Multi-domain]  Cd Length: 217  Bit Score: 129.03  E-value: 1.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  370 TCNCKKPDDD----TRKGCVDDCLNRMIFAECSPnTCPCGEQCCNQRIQRHEWVQcLERFRAEEKGWGIRTKEPLKAGQF 445
Cdd:cd10538     37 KCACAAESDGifayTKNGLLRLNNSPPPIFECNS-KCSCDDDCKNRVVQRGLQAR-LQVFRTSKKGWGVRSLEFIPKGSF 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  446 IIEYLGEVVSEQEFRNRMIEqYHNHSDHYCLNLDSGM---------VIDSYRMGNEARFINHSCDPNCEMQKWSVNG--- 513
Cdd:cd10538    115 VCEYVGEVITTSEADRRGKI-YDKSGGSYLFDLDEFSdsdgdgeelCVDATFCGNVSRFINHSCDPNLFPFNVVIDHddl 193

                          170       180
                   ....*....|....*....|....
gi 2462511422  514 -VYRIGLYALKDMPAGTELTYDYN 536
Cdd:cd10538    194 rYPRIALFATRDILPGEELTFDYG 217
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 431-556 1.72e-33

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380916  Cd Length: 150  Bit Score: 126.56  E-value: 1.72e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGEVVS-------EQEFRNRMIeqyhnhSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPN 503
Cdd:cd10518     25 GWGLFAKRPIAAGEMVIEYVGEVIRpivadkrEKRYDEEGG------GGTYMFRIDEDLVIDATKKGNIARFINHSCDPN 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  504 CEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSfnVEKQQL-CKCGFEKCR 556
Cdd:cd10518     99 CYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPI--EDEEKIpCLCGAPNCR 150
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
426-557 8.33e-32

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 121.22  E-value: 8.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  426 RAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHsdHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCE 505
Cdd:COG2940     12 PSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLH--TYLFELDDDGVIDGALGGNPARFINHSCDPNCE 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462511422  506 MqkWSVNGvyRIGLYALKDMPAGTELTYDYNFhsFNVEKQQLCKCGfeKCRG 557
Cdd:COG2940     90 A--DEEDG--RIFIVALRDIAAGEELTYDYGL--DYDEEEYPCRCP--NCRG 133
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 366-557 4.62e-31

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes.


Pssm-ID: 380915 [Multi-domain]  Cd Length: 288  Bit Score: 124.32  E-value: 4.62e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  366 YEATTCNCKKPDDDT---RKGCVDDCLNRMIFaECSPNtCPCGEQCCNQRIQRHEWVqCLERFRAEEKGWGIRTKEPLKA 442
Cdd:cd10517     75 IEATAATPGGQINPSagyQYRRLMEKLPTGVY-ECNSR-CKCDKRCYNRVVQNGLQV-RLQVFKTEKKGWGIRCLDDIPK 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  443 GQFIIEYLGEVVSEQEfrnrMIEQYHNHSDHYCLNLD------------------SGMVIDSYRMGNEARFINHSCDPNC 504
Cdd:cd10517    152 GSFVCIYAGQILTEDE----ANEEGLQYGDEYFAELDyievveklkegyesdveeHCYIIDAKSEGNLGRYLNHSCSPNL 227

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462511422  505 EMQKWSVNGV-YR---IGLYALKDMPAGTELTYDYNFHSFNVE-KQQLCKCGFEKCRG 557
Cdd:cd10517    228 FVQNVFVDTHdLRfpwVAFFASRYIRAGTELTWDYNYEVGSVPgKVLYCYCGSSNCRG 285
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 431-536 4.28e-30

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 115.31  E-value: 4.28e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGE-VVSEQEFRNRMIEQYHNHSDH------YCLNLDSGMVID--SYRMGNEARFINHSCD 501
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRlwgpylFTLDEDSEYCIDarALYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462511422  502 PNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYN 536
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 371-557 1.60e-27

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 methyltransferase Clr4, and similar proteins; This subfamily contains fission yeast Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (also known as Suv39h), the sole homolog of the mammalian SUV39H1 and SUV39H2 enzymes, that has a critical role in preventing aberrant heterochromatin formation. It is known to di- and tri-methylate Lys-9 of histone H3, a central heterochromatic histone modification, with its specificity profile most similar to that of the human SUV39H2 homolog.


Pssm-ID: 380999 [Multi-domain]  Cd Length: 259  Bit Score: 113.05  E-value: 1.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  371 CNCKKP-----DDDTRKGCVDD---------------CLNRMIFAECSPNtCPCGEQCCNQRIQRHEWVQcLERFRAEEK 430
Cdd:cd20073     26 CSCSKLggcdlNNPGSCQCLEDsneksfaydeygrvrANTGSIIYECNEN-CDCGINCPNRVVQRGRKLP-LEIFKTKHK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMiEQYHNHSDHYCLNLD-------SGMVIDSYRMGNEARFINHSCDPN 503
Cdd:cd20073    104 GWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRG-KKYDNVGVTYLFDLDlfedqvdEYYTVDAQYCGDVTRFINHSCDPN 182

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  504 CEMQKWSVN----GVYRIGLYALKDMPAGTELTYDY----NFHSF------------NVEKQQLCKCGFEKCRG 557
Cdd:cd20073    183 LAIYSVLRDksdsKIYDLAFFAIKDIPALEELTFDYsgrnNFDQLgfignrsnskyiNLKNKRPCYCGSANCRG 256
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 431-556 1.04e-26

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated.


Pssm-ID: 380946  Cd Length: 148  Bit Score: 107.04  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGEVV--SEQEFRNRMIEQYHNHSDhYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQK 508
Cdd:cd19169     24 DWGLFALEPIAADEMVIEYVGQVIrqSVADEREKRYEAIGIGSS-YLFRVDDDTIIDATKCGNLARFINHSCNPNCYAKI 102

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462511422  509 WSVNGVYRIGLYALKDMPAGTELTYDYNfhsFNVEKQQL-CKCGFEKCR 556
Cdd:cd19169    103 ITVESQKKIVIYSKRPIAVNEEITYDYK---FPIEDEKIpCLCGAPQCR 148
PHD_ASH1L cd15548
PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like ...
 861-903 1.29e-26

PHD finger found in histone-lysine N-methyltransferase ASH1L; ASH1L, also termed ASH1-like protein, or absent small and homeotic disks protein 1 homolog, or lysine N-methyltransferase 2H, is a protein belonging to the Trithorax family. It methylates Lys36 of histone H3 independently of transcriptional elongation to promote the establishment of Hox gene expression by counteracting Polycomb silencing. It can suppress interleukin-6 (IL-6), and tumor necrosis factor (TNF) production in Toll-like receptor (TLR)-triggered macrophages, and inflammatory autoimmune diseases by inducing the ubiquitin-editing enzyme A20. ASH1L contains an associated with SET domain (AWS), a SET domain, a post-SET domain, a bromodomain, a bromo-adjacent homology domain (BAH), and a plant homeodomain (PHD) finger.


Pssm-ID: 277023  Cd Length: 43  Bit Score: 102.93  E-value: 1.29e-26
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462511422  861 IRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQC 903
Cdd:cd15548      1 IRCICGLYKDEGLMIQCEKCMVWQHCDCMGVNDDVEHYLCEQC 43
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 396-557 4.71e-26

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), SET domain bifurcated 2 (SETDB2), and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380939 [Multi-domain]  Cd Length: 236  Bit Score: 108.01  E-value: 4.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  396 ECSPnTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSeqefRNRMIEQYHNHSDHYC 475
Cdd:cd10541     69 ECNK-LCKCDPNMCQNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILT----DDFADKEGLEMGDEYF 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  476 LNLD----SGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYR----IGLYALKDMPAGTELTYDYNFHSFNVE-KQQ 546
Cdd:cd10541    144 ANLDhieeSCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLrfpwVAFFASKRIKAGTELTWDYNYEVGSVEgKEL 223

                          170
                   ....*....|.
gi 2462511422  547 LCKCGFEKCRG 557
Cdd:cd10541    224 LCCCGSNECRG 234
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 381-557 1.31e-25

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; This subfamily contains Neurospora crassa DIM-5 (also termed H3-K9-HMTase dim-5, or HKMT) which functions as histone-lysine N-methyltransferase that specifically trimethylates histone H3 to form H3K9me3.


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 107.79  E-value: 1.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  381 RKGCV-DDCLN-RMIFAECSPnTCPCGEQCCNQRIQRHEWVqCLERFRAEE-KGWGIRTKEPLKAGQFIIEYLGEVVSEQ 457
Cdd:cd19473     66 KKGCLrGHMLNsRLPIYECHE-GCACSDDCPNRVVERGRKV-PLQIFRTSDgRGWGVRSTVDIKRGQFVDCYVGEIITPE 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  458 EF-RNRMIEQYHNHSDHYCLNLD--------------SGMVIDSYRMGNEARFINHSCDPNceMQKWSVNG------VYR 516
Cdd:cd19473    144 EAqRRRDAATIAQRKDVYLFALDkfsdpdsldprlrgDPYEIDGEFMSGPTRFINHSCDPN--LRIFARVGdhadkhIHD 221

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  517 IGLYALKDMPAGTELTYDY----------NFHSFNVEKQQLCKCGFEKCRG 557
Cdd:cd19473    222 LAFFAIKDIPRGTELTFDYvdgvtgldddAGDEEKEKEMTKCLCGSPKCRG 272
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 392-556 2.38e-25

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase EHMT1, EHMT2 and similar proteins; This family includes EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380941 [Multi-domain]  Cd Length: 231  Bit Score: 105.88  E-value: 2.38e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  392 MIFaECSPnTCPCGEQCCNQRIQRHewVQC-LERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmieqyhnH 470
Cdd:cd10543     66 LIF-ECNR-ACSCWRNCRNRVVQNG--IRYrLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSR-------E 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  471 SDHYCLNLDS----GMVIDSYRMGNEARFINHSCDPNCEMQKwsvngVY---------RIGLYALKDMPAGTELTYDYNF 537
Cdd:cd10543    135 DDSYLFDLDNkdgeTYCIDARRYGNISRFINHLCEPNLIPVR-----VFvehqdlrfpRIAFFASRDIKAGEELGFDYGE 209

                          170       180
                   ....*....|....*....|
gi 2462511422  538 HSFNVE-KQQLCKCGFEKCR 556
Cdd:cd10543    210 KFWRIKgKYFTCRCGSPKCK 229
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 368-537 3.83e-25

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar proteins; Arabidopsis thaliana SUVH protein (also termed suppressor of variegation 3-9 homolog protein) is a histone-lysine N-methyltransferase that methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. Some family members contain a post-SET domain which binds a Zn2+ ion. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380943 [Multi-domain]  Cd Length: 232  Bit Score: 105.18  E-value: 3.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  368 ATTCNCKKPDDDTRKGC----------VDDCLNRMIFA-----ECSPNtCPCGEQCCNQRIQRHEWVQcLERFRAEEKGW 432
Cdd:cd10545     21 STGCDCKNRCTDGASDCacvkknggeiPYNFNGRLIRAkpaiyECGPL-CKCPPSCYNRVTQKGLRYR-LEVFKTAERGW 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  433 GIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIeqyhnhSDHYCLNLD-------------------------------SG 481
Cdd:cd10545     99 GVRSWDSIPAGSFICEYVGELLDTSEADTRSG------NDDYLFDIDnrqtnrgwdggqrldvgmsdgerssaedeesSE 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  482 MVIDSYRMGNEARFINHSCDPNCEMQKWSV-NGVYRI---GLYALKDMPAGTELTYDYNF 537
Cdd:cd10545    173 FTIDAGSFGNVARFINHSCSPNLFVQCVLYdHNDLRLprvMLFAADNIPPLQELTYDYGY 232
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 431-537 3.02e-24

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380995  Cd Length: 120  Bit Score: 98.83  E-value: 3.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGEVVSEQEfRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWS 510
Cdd:cd19218     15 GWGIFIKDPVQKNEFISEYCGEIISQDE-ADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMM 93

                           90       100
                   ....*....|....*....|....*..
gi 2462511422  511 VNGVYRIGLYALKDMPAGTELTYDYNF 537
Cdd:cd19218     94 VNGDHRIGIFAKRAIQTGEELFFDYRY 120
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 432-556 6.63e-24

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces cerevisiae COMPASS complex and similar proteins; The family contains mostly fungal SET domains, including SET1 found in the catalytic component of the Saccharomyces cerevisiae COMPASS (complex of proteins associated with Set1). SET1 is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex. The activity of this catalytic domain is established through forming a complex with a set of core proteins; it is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3).


Pssm-ID: 380998  Cd Length: 148  Bit Score: 99.04  E-value: 6.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  432 WGIRTKEPLKAGQFIIEYLGEVVSEQ--EFRNRMIEQYHNHSDhYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKW 509
Cdd:cd20072     25 WGLYAMENISAKDMVIEYVGEVIRQQvaDEREKRYLRQGIGSS-YLFRIDDDTVVDATKKGNIARFINHCCDPNCTAKII 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462511422  510 SVNGVYRIGLYALKDMPAGTELTYDYNFHSfnVEKQQLCKCGFEKCR 556
Cdd:cd20072    104 KVEGEKRIVIYAKRDIAAGEELTYDYKFPR--EEDKIPCLCGAPNCR 148
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 425-557 1.26e-23

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins; This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 98.23  E-value: 1.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  425 FRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmiEQYHNHSDHYC--LNLDSGMVIDSYRMGNEARFINHSCDP 502
Cdd:cd19170     19 YRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKR--EKYYESKGIGCymFRIDDDEVVDATMHGNAARFINHSCEP 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462511422  503 NCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNfhsFNVEKQQL-CKCGFEKCRG 557
Cdd:cd19170     97 NCYSRVVNIDGKKHIVIFALRRILRGEELTYDYK---FPIEDVKIpCTCGSKKCRK 149
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 433-537 5.54e-23

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380927  Cd Length: 127  Bit Score: 95.42  E-value: 5.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  433 GIRTKEPLKAGQFIIEYLGEVVSEQEFR--NRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWS 510
Cdd:cd10529     18 GLVATEDISPGEPILEYKGEVSLRSEFKedNGFFKRPSPFVFFYDGFEGLPLCVDARKYGNEARFIRRSCRPNAELRHVV 97

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462511422  511 V-NGVYRIGLYALKDMPAGTELT--YDYNF 537
Cdd:cd10529     98 VsNGELRLFIFALKDIRKGTEITipFDYDY 127
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
 429-535 1.04e-22

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380945  Cd Length: 124  Bit Score: 94.56  E-value: 1.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  429 EKGWGIRTKEPLKAGQFIIEYLGEVVSEQEfRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDP----NC 504
Cdd:cd19168     11 ECGLGLFAAEDIKEGEFVIEYTGELISHDE-GVRREHRRGDVSYLYLFEEQEGIWVDAAIYGNLSRYINHATDKvktgNC 89

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462511422  505 EMQKWSVNGVYRIGLYALKDMPAGTELTYDY 535
Cdd:cd19168     90 MPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 396-557 9.53e-22

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 2 (SUV39H2) and similar proteins; SUV39H2 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B (KMT1B), or Su(var)3-9 homolog 2) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 95.73  E-value: 9.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  396 ECSpNTCPCGEQCCNQRIQR-HEWVQCLerFRAEE-KGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMiEQYHNHSDH 473
Cdd:cd10532     62 ECN-SRCKCGPDCPNRVVQKgTQYSLCI--FRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRG-QFYDSKGIT 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  474 YCLNLD---SGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNG----VYRIGLYALKDMPAGTELTYDY----------- 535
Cdd:cd10532    138 YLFDLDyesDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNldtrLPRIALFSTRTIKAGEELTFDYqmkgsgdlssd 217

                          170       180
                   ....*....|....*....|....
gi 2462511422  536 --NFHSFNVEKQQLCKCGFEKCRG 557
Cdd:cd10532    218 siDNSPAKKRVRTVCKCGAVTCRG 241
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 430-536 4.96e-21

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 89.71  E-value: 4.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  430 KGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmiEQYHNHSDhYCLNLDSGM-VIDSYRMGNEARFINHSCDPNCEMQK 508
Cdd:cd10522     13 NGLGLFAAETIAKGEFVGEYTGEVLDRWEEDRD--SVYHYDPL-YPFDLNGDIlVIDAGKKGNLTRFINHSDQPNLELIV 89

                           90       100
                   ....*....|....*....|....*...
gi 2462511422  509 WSVNGVYRIGLYALKDMPAGTELTYDYN 536
Cdd:cd10522     90 RTLKGEQHIGFVAIRDIKPGEELFISYG 117
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 396-556 5.04e-21

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 1 (SUV39H1) and similar proteins; SUV39H1 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A (KMT1A), position-effect variegation 3-9 homolog (SUV39H), or Su(var)3-9 homolog 1) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 94.19  E-value: 5.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  396 ECSpNTCPCGEQCCNQRIQRH-EWVQCLerFRAEE-KGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMiEQYHNHSDH 473
Cdd:cd10525     64 ECN-SRCRCGPDCPNRVVQKGiQYDLCI--FRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRG-QIYDRQGAT 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  474 YCLNLD---SGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNG----VYRIGLYALKDMPAGTELTYDYNFH--SFNVEK 544
Cdd:cd10525    140 YLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNlderLPRIALFATRTIRAGEELTFDYNMQvdPVDAES 219

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462511422  545 QQL--------------------CKCGFEKCR 556
Cdd:cd10525    220 TKMdsnfglaglpgspkkrvrieCKCGVRSCR 251
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 431-537 7.27e-21

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43), also termed ENX-2, or histone-lysine N-methyltransferase EZH1, is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380994  Cd Length: 136  Bit Score: 89.74  E-value: 7.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  431 GWGIRTKEPLKAGQFIIEYLGEVVSEQEfRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWS 510
Cdd:cd19217     17 GWGTFIKESVQKNEFISEYCGELISQDE-ADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVM 95

                           90       100
                   ....*....|....*....|....*..
gi 2462511422  511 VNGVYRIGLYALKDMPAGTELTYDYNF 537
Cdd:cd19217     96 VNGDHRIGIFAKRAIQQGEELFFDYRY 122
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 425-556 1.22e-20

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins; KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac).


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 89.70  E-value: 1.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  425 FRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmiEQYHNHSDHYC--LNLDSGMVIDSYRMGNEARFINHSCDP 502
Cdd:cd19206     19 YRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKR--EKYYDSKGIGCymFRIDDSEVVDATMHGNAARFINHSCEP 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  503 NCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCR 556
Cdd:cd19206     97 NCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCR 150
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 392-556 2.30e-20

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 2 (EHMT2) and similar proteins; EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C (KMT1C), or protein G9a) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380931 [Multi-domain]  Cd Length: 239  Bit Score: 91.62  E-value: 2.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  392 MIFaECSpNTCPCGEQCCNQRIQRHEWVQcLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmieqyhnHS 471
Cdd:cd10533     66 LIF-ECN-QACSCWRNCKNRVVQSGIKVR-LQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR-------ED 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  472 DHYCLNLDS--GMV--IDSYRMGNEARFINHSCDPN-----CEMQKWSVNgVYRIGLYALKDMPAGTELTYDYNFHSFNV 542
Cdd:cd10533    136 DSYLFDLDNkdGEVycIDARYYGNISRFINHLCDPNiipvrVFMLHQDLR-FPRIAFFSSRDIRTGEELGFDYGDRFWDI 214

                          170
                   ....*....|....*
gi 2462511422  543 EKQQL-CKCGFEKCR 556
Cdd:cd10533    215 KSKYFtCQCGSEKCK 229
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 392-556 3.12e-20

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 91.15  E-value: 3.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  392 MIFaECSpNTCPCGEQCCNQRIQRHEWVQcLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmieqyhnHS 471
Cdd:cd10535     66 LIF-ECN-HACSCWRNCRNRVVQNGLRAR-LQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVR-------EE 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  472 DHYCLNLDS--GMV--IDSYRMGNEARFINHSCDPN-----CEMQKWSVNgVYRIGLYALKDMPAGTELTYDYNFHSFNV 542
Cdd:cd10535    136 DSYLFDLDNkdGEVycIDARFYGNVSRFINHHCEPNlvpvrVFMAHQDLR-FPRIAFFSTRLIEAGEQLGFDYGERFWDI 214

                          170
                   ....*....|....*
gi 2462511422  543 EKQQL-CKCGFEKCR 556
Cdd:cd10535    215 KGKLFsCRCGSPKCR 229
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 724-820 3.43e-20

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 86.66  E-value: 3.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  724 FKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGR 803
Cdd:cd04369      1 LKKKLRSLLDALKKLKRDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGP 80

                           90
                   ....*....|....*..
gi 2462511422  804 KSPVGRDVCRLRKAYYN 820
Cdd:cd04369     81 GSPIYKDAKKLEKLFEK 97
BROMO smart00297
bromo domain;
719-816 7.16e-20

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 85.79  E-value: 7.16e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422   719 RLAQIFKEICDGIISYKDSSRqaLAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAE 798
Cdd:smart00297    3 KLQKKLQELLKAVLDKLDSHP--LSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNAR 80

                            90
                    ....*....|....*...
gi 2462511422   799 KYYGRKSPVGRDVCRLRK 816
Cdd:smart00297   81 TYNGPDSEVYKDAKKLEK 98
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 415-557 1.42e-19

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


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 86.71  E-value: 1.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  415 RHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVsEQEFRNRMIEQY--HNHSDhYCLNLDSGMVIDSYRMGNE 492
Cdd:cd19171      9 KTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEII-RNEVANRREKIYesQNRGI-YMFRIDNDWVIDATMTGGP 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422  493 ARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCRG 557
Cdd:cd19171     87 ARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRK 151
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 424-559 2.62e-19

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and similar proteins; SETD1A (EC2.1.1.43), also termed lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit SET1, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Human SET domain containing protein 1A (hSETD1A) expression occurs at a high rate in hepatocellular carcinoma patients and controls tumor metastasis in breast cancer by activating MMP expression.


Pssm-ID: 380981 [Multi-domain]  Cd Length: 153  Bit Score: 85.85  E-value: 2.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  424 RF-RAEEKGWGIRTKEPLKAGQFIIEYLGEVVSE--QEFRNRMIEQyHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSC 500
Cdd:cd19204     17 RFgRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQvvADMREKRYVQ-EGIGSSYLFRVDHDTIIDATKCGNLARFINHCC 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  501 DPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNfhsFNVEKQQL-CKCGFEKCRGII 559
Cdd:cd19204     96 TPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYK---FPIEDNKIpCLCGTENCRGTL 152
BAH smart00439
Bromo adjacent homology domain;
941-1072 3.50e-19

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 84.65  E-value: 3.50e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422   941 GDCVYLMRDSRRTPdghpvrqsyrllshinrdkLDIFRIEKLW--KNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFR 1018
Cdd:smart00439    5 GDFVLVEPDDADEP-------------------YYIGRIEEIFetKKNSESKMVRVRWFYRPEETVLEKAALFDKNEVFL 65

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422  1019 VPLYEIIPLEAVVGTCCVLDLYTYCKGRPKGV-KEQDVYICDYRLDKSAHLFYKI 1072
Cdd:smart00439   66 SDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSiGEPDVFFCESAYDPEKGSFKKL 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 941-1072 7.84e-19

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 83.51  E-value: 7.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  941 GDCVYLmrdsrrtpDGHPVRQSYRllshinrdkldIFRIEKLWKNEKEERF-AFGHHYFRPHETHHSPSRRFYHNELFRV 1019
Cdd:pfam01426    6 GDFVLV--------EPDDADEPYY-----------VARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLS 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462511422 1020 PLYEIIPLEAVVGTCCVLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKI 1072
Cdd:pfam01426   67 DEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKEPDDFFCELLYDPKTKSFKKL 119
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 426-559 1.79e-18

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins; SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 83.57  E-value: 1.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  426 RAEEKGWGIRTKEPLKAGQFIIEYLGEVVSE--QEFRNRMIEQyHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPN 503
Cdd:cd19205     20 KSHIHDWGLFAMEPIAADEMVIEYVGQNIRQviADMREKRYED-EGIGSSYMFRVDHDTIIDATKCGNFARFINHSCNPN 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462511422  504 CEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNfhsFNVEKQQL-CKCGFEKCRGII 559
Cdd:cd19205     99 CYAKVITVESQKKIVIYSKQHINVNEEITYDYK---FPIEDVKIpCLCGSENCRGTL 152
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 396-559 5.43e-18

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) and similar proteins; SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380921 [Multi-domain]  Cd Length: 266  Bit Score: 85.27  E-value: 5.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  396 ECSPnTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSeqefrnRMIEQYHNHSDHYC 475
Cdd:cd10523     85 ECNV-SCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLS------RARSPTEPLPPKLE 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  476 LNLDSGM--------------------VIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYR----IGLYALKDMPAGTEL 531
Cdd:cd10523    158 LPSENEVevvtswlilskkrklrenvcFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTEL 237

                          170       180
                   ....*....|....*....|....*....
gi 2462511422  532 TYDYNFHSFNV-EKQQLCKCGFEKCRGII 559
Cdd:cd10523    238 TWDYSYDAGTSpEQEIPCLCGVNKCQKKI 266
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 430-536 9.08e-18

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 78.83  E-value: 9.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  430 KGWGIRTKEPLKAGQFIIEylgevvseqefrnrmieqyhnhsdhyclnldsgmvidsyrmgneARFINHSCDPNCEMQKW 509
Cdd:cd08161     10 AGFGLFATRDIPKGEVIGL--------------------------------------------ARFINHSCEPNCEFEEV 45

                           90       100
                   ....*....|....*....|....*..
gi 2462511422  510 SVNGVYRIGLYALKDMPAGTELTYDYN 536
Cdd:cd08161     46 YVGGKPRVFIVALRDIKAGEELTVDYG 72
AWS smart00570
associated with SET domains; subdomain of PRESET
 367-418 1.03e-17

associated with SET domains; subdomain of PRESET


Pssm-ID: 197795  Cd Length: 50  Bit Score: 77.83  E-value: 1.03e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2462511422   367 EATTCNCKKPDDDtRKGCVDDCLNRMIFAECsPNTCPCGEQCCNQRIQRHEW 418
Cdd:smart00570    1 DIMTCECKPTDDD-ETACGSDCLNRMLFIEC-SSSCPCGSYCSNQRFQKRQY 50
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 425-556 1.68e-17

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins; KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation.


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 80.84  E-value: 1.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  425 FRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRmiEQYHNHSDHYC--LNLDSGMVIDSYRMGNEARFINHSCDP 502
Cdd:cd19207     19 YRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKR--EKFYDSKGIGCymFRIDDFDVVDATMHGNAARFINHSCEP 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  503 NCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCR 556
Cdd:cd19207     97 NCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCR 150
AWS pfam17907
AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...
 378-416 3.06e-17

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc binding domain. The full AWS domain contains 8 cysteines. This entry represents the N-terminal part of the domain, with the C-terminal part interwoven with the SET domain.


Pssm-ID: 465559  Cd Length: 39  Bit Score: 76.31  E-value: 3.06e-17
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462511422  378 DDTRKGCVDDCLNRMIFAECSPNTCPCGEQCCNQRIQRH 416
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
 862-903 6.28e-17

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 75.43  E-value: 6.28e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462511422  862 RCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDV--EHYLCEQC 903
Cdd:cd15550      1 RCICGFEHDDGFMICCDKCSVWQHGDCMGIDRENipDSYLCEQC 44
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 411-535 1.43e-16

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2.1.1.43; also termed N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, lysine N-methyltransferase 5A, lysine-specific methylase 5A, PR/SET domain-containing protein 07, PR-Set7 or PR/SET07) is a nucleosomal histone-lysine N-methyltransferase that specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). It plays a central role in the silencing of euchromatic genes.


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 77.62  E-value: 1.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  411 QRIQRHEWVqCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSD----HYCLNLDSGMVID- 485
Cdd:cd10528      9 ELILSGKEE-GLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYAKDPSTgcymYYFQYKGKTYCVDa 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  486 ---SYRMGneaRFINHSC-DPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDY 535
Cdd:cd10528     88 tkeSGRLG---RLINHSKkKPNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 412-556 1.44e-15

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380986 [Multi-domain]  Cd Length: 155  Bit Score: 75.50  E-value: 1.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  412 RIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVsEQEFRNRMIEQYHNHSDH-YCLNLDSGMVIDSYRMG 490
Cdd:cd19209      8 RRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTII-RNEVANRREKIYEEQNRGiYMFRINNEHVIDATLTG 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462511422  491 NEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCR 556
Cdd:cd19209     87 GPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCR 152
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 719-822 5.73e-15

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 72.08  E-value: 5.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  719 RLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAE 798
Cdd:cd05516      1 ELTKKMNKIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80

                           90       100
                   ....*....|....*....|....
gi 2462511422  799 KYYGRKSPVGRDVCRLRKAYYNAR 822
Cdd:cd05516     81 TFNLEGSLIYEDSIVLQSVFKSAR 104
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 726-824 3.38e-14

Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 70.05  E-value: 3.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  726 EICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKS 805
Cdd:cd05524      9 ELYDTIRNYKSEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDS 88

                           90
                   ....*....|....*....
gi 2462511422  806 PVGRDVCRLRKAYYNARHE 824
Cdd:cd05524     89 PEHKDACKLWELFLSARNE 107
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
 412-556 5.96e-14

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C (EC2.1.1.43; also termed lysine N-methyltransferase 2C, homologous to ALR protein (HALR) myeloid/lymphoid, or mixed-lineage leukemia protein 3 (MLL3)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me) and may be involved in leukemogenesis and developmental disorder. KMT2C is a catalytic subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. Overexpression of KMT2C is associated with estrogen receptor-positive breast cancer; KMT2C mediates the estrogen dependence of breast cancer through regulation of estrogen receptor alpha (ERalpha) enhancer function. KMT2C is frequently mutated in certain populations with diffuse-type gastric adenocarcinomas (DGA); its loss promotes epithelial-to-mesenchymal transition (EMT) and is associated with worse overall survival.


Pssm-ID: 380985 [Multi-domain]  Cd Length: 154  Bit Score: 70.81  E-value: 5.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  412 RIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVsEQEFRNRMIEQYHNHSDH-YCLNLDSGMVIDSYRMG 490
Cdd:cd19208      7 RKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTII-RNEVANRKEKLYESQNRGvYMFRIDNDHVIDATLTG 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462511422  491 NEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCR 556
Cdd:cd19208     86 GPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCR 151
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 433-545 6.17e-14

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins; Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression.


Pssm-ID: 380960  Cd Length: 173  Bit Score: 71.28  E-value: 6.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  433 GIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQY----------HNHSDhyclnldSGMVIDSYRMGNEARFINHSCDP 502
Cdd:cd19183     15 GLFADRPIPAGDPIQELLGEIGLQSEYIADPENQYqilgapkphvFFHPQ-------SPLYIDTRRSGSVARFIRRSCRP 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462511422  503 NCEMQ--KWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQ 545
Cdd:cd19183     88 NAELVtvASDSGSVLKFVLYASRDISPGEEITIGWDWDNPHPFRR 132
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 728-813 2.48e-13

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 66.57  E-value: 2.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  728 CDGIISYKDssRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPV 807
Cdd:pfam00439    1 CLEILDKLM--EHPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVI 78


                   ....*.
gi 2462511422  808 GRDVCR 813
Cdd:pfam00439   79 YKAAEK 84
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 720-824 1.49e-12

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 65.02  E-value: 1.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  720 LAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEK 799
Cdd:cd05515      1 MQQKLWELYNAVKNYTDGRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACK 80

                           90       100
                   ....*....|....*....|....*
gi 2462511422  800 YYGRKSPVGRDVCRLRKAYYNARHE 824
Cdd:cd05515     81 YNEPDSQIYKDALTLQKVLLETKRE 105
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 729-817 2.41e-12

Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99951  Cd Length: 103  Bit Score: 64.28  E-value: 2.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  729 DGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVG 808
Cdd:cd05520     10 DTIRNARNNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIY 89


                   ....*....
gi 2462511422  809 RDVCRLRKA 817
Cdd:cd05520     90 KDAEKLQKL 98
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 412-555 4.20e-11

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression.


Pssm-ID: 380958  Cd Length: 150  Bit Score: 62.33  E-value: 4.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  412 RIQRHEWVqclerfraeekgwgIRTKEPLKAGQFIIEYLGEVVSEQEFR--NRMIEQYHNHSDHYCLNLDSGMVIDSYRM 489
Cdd:cd19181     13 RVQKHRKI--------------LRAARDLALDTLIIEYRGKVMLRQQFEvnGHFFKRPYPFVLFYSKFNGVEMCVDARTF 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462511422  490 GNEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELT--YDYNFHSFNVEKQQLCKCGFEKC 555
Cdd:cd19181     79 GNDARFIRRSCTPNAEVRHMIADGMIHLCIYAVAAIAKDAEVTiaFDYEYSNCNYKVDCACHKGNRNC 146
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 731-817 6.23e-11

Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 60.54  E-value: 6.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  731 IISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRD 810
Cdd:cd05518     12 VLEYREGSGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVYED 91


                   ....*..
gi 2462511422  811 VCRLRKA 817
Cdd:cd05518     92 ANILEKV 98
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 757-821 2.64e-10

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 58.33  E-value: 2.64e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422  757 DYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRDVCRLRKAYYNA 821
Cdd:cd05509     33 DYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTEYYKCANKLEKFFWKK 97
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 747-818 4.05e-10

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99932  Cd Length: 103  Bit Score: 58.09  E-value: 4.05e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462511422  747 LNLPpkkknaDYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRDVCRLRKAY 818
Cdd:cd05500     34 LNIP------HYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 495-555 4.95e-10

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


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 58.54  E-value: 4.95e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  495 FINHSCDPNCEmqkWSVNGVYRIGLYALKDMPAGTELTYDY--NFHSFNVEKQQL-------CKCgfEKC 555
Cdd:cd20071     58 LLNHSCDPNAV---VVFDGNGTLRVRALRDIKAGEELTISYidPLLPRTERRRELlekygftCSC--PRC 122
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 720-817 5.82e-10

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 57.73  E-value: 5.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  720 LAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEK 799
Cdd:cd05519      1 LKAAMLEIYDAVLNCEDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANART 80

                           90
                   ....*....|....*...
gi 2462511422  800 YYGRKSPVGRDVCRLRKA 817
Cdd:cd05519     81 YNQEGSIVYEDAVEMEKA 98
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 720-816 1.44e-09

Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99948  Cd Length: 103  Bit Score: 56.29  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  720 LAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEK 799
Cdd:cd05517      1 LKQILEQLLEAVMTATDPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKT 80

                           90
                   ....*....|....*..
gi 2462511422  800 YYGRKSPVGRDVCRLRK 816
Cdd:cd05517     81 FNEPGSQVYKDANAIKK 97
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 718-810 1.68e-09

Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 56.48  E-value: 1.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  718 ARLAQIFKeicdGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNA 797
Cdd:cd05522      4 ARIKNILK----GLRKERDENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENA 79

                           90
                   ....*....|...
gi 2462511422  798 EKYYGRKSPVGRD 810
Cdd:cd05522     80 KLYNENDSQEYKD 92
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 747-811 1.75e-09

Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99938  Cd Length: 99  Bit Score: 56.18  E-value: 1.75e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422  747 LNLPpkkknaDYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYygrkSPVGRDV 811
Cdd:cd05506     30 LGLP------DYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRY----NPPGNDV 84
PHD_Bye1p_SIZ1_like cd15570
PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo ...
 862-903 2.20e-09

PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo Ligase SIZ1, and similar proteins; Yeast Bye1p is a nuclear transcription factor with a domain resembling the central domain in the transcription elongation factor TFIIS and plays an inhibitory role during transcription elongation. It functions as a multicopy suppressor of Ess1, a peptidyl-prolyl cis-trans isomerase involved in proline isomerization of the C-terminal domain (CTD) of RNA polymerase II (Pol II). Bye1p contains an N-terminal plant homeodomain (PHD) finger, a central Pol II-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. The PHD domain binds to a histone H3 tail peptide containing trimethylated lysine 4 (H3K4me3). The TLD domain is responsible for the association with chromatin. Plant SIZ1 protein is a SUMO (small ubiquitin-related modifier) E3 ligase that facilitates conjugation of SUMO to substrate target proteins (sumoylation) and belongs to the protein inhibitor of activated STAT (PIAS) protein family. It negatively regulates abscisic acid (ABA) signaling, which is dependent on the bZIP transcripton factor ABI5. It also modulates plant growth and plays a role in drought stress response likely through the regulation of gene expression. SIZ1 functions as a floral repressor that not only represses the salicylic acid (SA)-dependent pathway, but also promotes FLOWERING LOCUS C (FLC) expression by repressing FLOWERING LOCUS D (FLD) activity through sumoylation. SIZ1 contains a PHD finger, which specifically binds methylated histone H3 at lysine 4 and arginine 2.


Pssm-ID: 277045  Cd Length: 50  Bit Score: 54.39  E-value: 2.20e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462511422  862 RCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDV--------EHYLCEQC 903
Cdd:cd15570      1 RCPCGSSMEDGSMIQCEGCKTWQHMDCVLIPDKPadglpelpSKFYCELC 50
PHD_PHF20L1 cd15633
PHD finger found in PHD finger protein 20-like protein 1 (P20L1); P20L1 is an active malignant ...
 862-903 2.24e-09

PHD finger found in PHD finger protein 20-like protein 1 (P20L1); P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.


Pssm-ID: 277103  Cd Length: 46  Bit Score: 54.26  E-value: 2.24e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462511422  862 RCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDV--EHYLCEQC 903
Cdd:cd15633      1 RCICEMDEENGFMIQCEECLCWQHSVCMGLLEESipEQYICYIC 44
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
 417-536 5.06e-09

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The family includes Arabidopsis thaliana ATXR5 and ATXR6. Both ATXR5 (also termed protein SET DOMAIN GROUP 15, or TRX-related protein 5) and ATXR6 (also termed protein SET DOMAIN GROUP 34, or TRX-related protein 6) function as histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). They are required for chromatin structure and gene silencing.


Pssm-ID: 380937  Cd Length: 138  Bit Score: 55.88  E-value: 5.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  417 EWVQCLERFRAEEkGWGIRTKEPLKAGQFIIEYLGEVvseQEFRNRmiEQYHNHSDHYCL---NLDSGMVIDSYRMGNEA 493
Cdd:cd10539      2 ECPPLLVVFDPRE-GFTVEADGFIKDLTIIAEYTGDV---DYIRNR--EFDDNDSIMTLLlagDPSKSLVICPDKRGNIA 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  494 RFI----NHSCD----PNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYN 536
Cdd:cd10539     76 RFIsginNHTKDgkkkQNCKCVRYSINGEARVLLVATRDIAKGERLYYDYN 126
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 719-810 6.75e-09

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 59.43  E-value: 6.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  719 RLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAE 798
Cdd:COG5076    142 LLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCK 221

                           90
                   ....*....|..
gi 2462511422  799 KYYGRKSPVGRD 810
Cdd:COG5076    222 LYNGPDSSVYVD 233
PHD_MMD1_like cd15556
PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD ...
 863-903 1.08e-08

PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD finger protein MALE STERILITY 1 (MS1), and similar proteins; MMD1 is a plant homeodomain (PHD) finger protein expressed in male meiocytes. It is encoded by the gene DUET, which is required for male meiotic chromosome organization and progression. MMD1 has been implicated in the regulation of gene expression during meiosis. The mmd1 mutation triggers cell death in male meiocytes. MS1 is a nuclear transcriptional activator that is important for tapetal development and pollen wall biosynthesis. It contains a Leu zipper-like domain and a PHD finger motif, both of which are essential for its function.


Pssm-ID: 277031 [Multi-domain]  Cd Length: 46  Bit Score: 52.00  E-value: 1.08e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462511422  863 CICGLYKDEG-LMIQCDKCMVWQHCDCMGVNSDVE---HYLCEQC 903
Cdd:cd15556      2 CSCGTRDDDGeRMIACDVCEVWQHTRCVGIADNEEppdHFLCRRC 46
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 752-806 1.30e-08

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 54.19  E-value: 1.30e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422  752 KKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSP 806
Cdd:cd05511     27 KKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSV 81
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
 435-537 1.37e-08

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide.


Pssm-ID: 380959  Cd Length: 129  Bit Score: 54.51  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  435 RTKEPLKAGQ------FIIEYLGEVVSEQEFR------NRMIEQYHNHSDHYCLNldsgMVIDSYRMGNEARFINHSCDP 502
Cdd:cd19182     16 KNKKILKAAKdlppdtLIIEYRGKFMLREQFEangyffKRPYPFVLFYSKFHGLE----MCVDARTFGNEARFIRRSCTP 91

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462511422  503 NCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNF 537
Cdd:cd19182     92 NAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDF 126
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 967-1069 1.48e-08

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 54.32  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  967 SHINRDKLDIFRIEKLWKNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFRVPLYEIIPLEAVVGTCCVLDLYTYCKG- 1045
Cdd:cd04370     16 DSIKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALRRELFLSDHLDEIPVESIIGKCKVLFVSEFEGLk 95

                           90       100
                   ....*....|....*....|....
gi 2462511422 1046 RPKGVKEQDVYICDYRLDKSAHLF 1069
Cdd:cd04370     96 QRPNKIDTDDFFCRLAYDPTTKEF 119
PHD_PHF20_like cd15549
PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 ...
 862-903 3.74e-08

PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 (P20L1); PHF20, also termed Glioma-expressed antigen 2, or hepatocellular carcinoma-associated antigen 58, or novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53 mediated signaling. P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. Both PHF20 and PHF20L1 contain an N-terminal MBT domain, two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.


Pssm-ID: 277024  Cd Length: 45  Bit Score: 50.55  E-value: 3.74e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462511422  862 RCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSD---VEHYLCEQC 903
Cdd:cd15549      1 HCICGVNEENGLMIQCELCLCWQHGVCMGIEEEesvPERYVCYVC 45
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 725-807 4.75e-08

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 52.15  E-value: 4.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  725 KEICDGIIS----YKDSSrqalaaPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKY 800
Cdd:cd05505      2 LQKCEEILSkilkYRFSW------PFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKY 75


                   ....*..
gi 2462511422  801 YGRKSPV 807
Cdd:cd05505     76 YENGSYV 82
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 758-822 6.98e-08

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 51.61  E-value: 6.98e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462511422  758 YYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRDVCRLRKaYYNAR 822
Cdd:cd05503     33 YRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRK-FFEKR 96
PHD_PHF20 cd15634
PHD finger found in PHD finger protein 20 (PHF20); PHF20, also termed Glioma-expressed antigen ...
 862-903 2.08e-07

PHD finger found in PHD finger protein 20 (PHF20); PHF20, also termed Glioma-expressed antigen 2, or hepatocellular carcinoma-associated antigen 58, or novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53 mediated signaling. PHF20 contains an N-terminal malignant brain tumor (MBT) domain, two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.


Pssm-ID: 277104  Cd Length: 44  Bit Score: 48.40  E-value: 2.08e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462511422  862 RCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSD--VEHYLCEQC 903
Cdd:cd15634      1 RCICEVQEENDFMIQCEECLCWQHGVCMGLLEDnvPEKYTCYIC 44
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 745-816 3.59e-07

Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99936  Cd Length: 115  Bit Score: 50.09  E-value: 3.59e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462511422  745 PLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRDVCRLRK 816
Cdd:cd05504     32 PFLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQR 103
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 728-812 4.23e-07

Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99930  Cd Length: 102  Bit Score: 49.58  E-value: 4.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  728 CDGIISYKDSSR-QALAAPLLNL--PPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYygrk 804
Cdd:cd05498      5 CSGILKELFSKKhKAYAWPFYKPvdPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKY---- 80


                   ....*...
gi 2462511422  805 SPVGRDVC 812
Cdd:cd05498     81 NPPDHPVH 88
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 863-906 4.33e-07

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 47.87  E-value: 4.33e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462511422  863 CICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVE-----HYLCEQCDPR 906
Cdd:pfam00628    3 AVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAeipsgEWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 863-903 6.89e-07

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 47.21  E-value: 6.89e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 2462511422   863 CICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDV----EHYLCEQC 903
Cdd:smart00249    3 SVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeepdGKWYCPKC 47
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 757-843 7.04e-07

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 48.89  E-value: 7.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  757 DYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRdvcrlrkayyNARHEASAQIDEIVGET 836
Cdd:cd05528     35 DYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNPDRDPADK----------LIRSRACELRDEVHAMI 104


                   ....*..
gi 2462511422  837 ASEADSS 843
Cdd:cd05528    105 EAELDPL 111
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 750-810 3.54e-06

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 46.90  E-value: 3.54e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  750 PPKKKNADYYEKISDPLDLITIEKQI---LTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRD 810
Cdd:cd05502     28 PVSPSVPNYYKIIKTPMDLSLIRKKLqpkSPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQA 91
PHD_PHF2_like cd15554
PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar ...
 863-903 6.99e-06

PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar proteins. PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20(H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. All family members contain a plant homeodomain (PHD) finger and a JmjC domain.


Pssm-ID: 277029  Cd Length: 47  Bit Score: 44.30  E-value: 6.99e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462511422  863 CICGL-YKDEGLMIQCDKCMVWQHCDCMGVN----SDVEHYLCEQC 903
Cdd:cd15554      2 CICRQpYDVTRFMIECDVCKDWFHGSCVGVEehqaNDIERYHCPNC 47
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 493-556 1.01e-05

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


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 46.51  E-value: 1.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  493 ARFINHSCDPNCemqKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQlCKCgfEKCR 556
Cdd:cd10524     77 AAFINHDCRPNC---KFVPTGKSTACVKVLRDIEPGEEITVYYGDNYFGENNEE-CEC--ETCE 134
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 422-541 1.19e-05

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


Pssm-ID: 380938  Cd Length: 112  Bit Score: 45.71  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  422 LERFRAEEKGWGIRTKEPLKAGQFIieylgEVVSEQEFRNrmieQYHNHS-----DHYClnldsgmvidsYRMGNEARFI 496
Cdd:cd10540      2 LEVKPSTLKGRGVFATRPIKKGEVI-----EEAPVIVLPK----EEYQHLcktvlDHYV-----------FSWGDGCLAL 61

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462511422  497 --------NHSCDPNCEMQKWSVNGvyRIGLYALKDMPAGTELTYDYNFHSFN 541
Cdd:cd10540     62 algygsmfNHSYTPNAEYEIDFENQ--TIVFYALRDIEAGEELTINYGDDLWD 112
PHD_Hop1p_like cd15558
PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and ...
 862-894 1.36e-05

PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and similar proteins; Fission yeast Hop1p, also termed linear element-associated protein hop1, is an S. pombe homolog of the synaptonemal complex (SC)-associated protein Hop1 in Saccharomyces cerevisiae. In contrast to S. cerevisiae, S. pombe forms thin threads, known as linear elements (LinEs), in meiotic nuclei, instead of a canonical synaptonemal complex. LinEs contain Rec10 protein and are evolutionary relics of SC axial elements. Fission yeast Hop1p is a linear element (LinE)-associated protein. It also associates with Rec10, which plays a role in recruiting the recombination machinery to chromatin. Hop1p contains an N-terminal HORMA (for Hop1p, Rev7p, and MAD2) domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277033  Cd Length: 47  Bit Score: 43.59  E-value: 1.36e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462511422  862 RCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSD 894
Cdd:cd15558      1 RCECGDWGEDGAMIQCAFCDTWQHLLCYGFESA 33
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 757-809 1.45e-05

Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99958  Cd Length: 128  Bit Score: 45.79  E-value: 1.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462511422  757 DYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGR 809
Cdd:cd05529     60 DYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEIAK 112
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 724-816 6.00e-05

Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 43.58  E-value: 6.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  724 FKEICDGIIS-YKDSSRQALaaPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYG 802
Cdd:cd05510      8 FYESLDKVLNeLKTYTEHST--PFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYNS 85

                           90
                   ....*....|....*
gi 2462511422  803 RKS-PVGRDVCRLRK 816
Cdd:cd05510     86 DPShPLRRHANFMKK 100
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 863-903 6.57e-05

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 41.53  E-value: 6.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462511422  863 CICGL-YKDEGLMIQCDKCMVWQHCDCMGVNS----DVEHYLCEQC 903
Cdd:cd15489      3 IVCGKgGDLGGELLQCDGCGKWFHADCLGPPLssfvPNGKWICPVC 48
PHD_Cfp1 cd15553
PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding ...
 863-903 6.83e-05

PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding protein, or PHD finger and CXXC domain-containing protein 1 (PCCX1), is a specificity factor that binds to unmethylated CpGs and links H3K4me3 with CpG islands (CGIs). It integrates both promoter CpG content and gene activity for accurate trimethylation of histone H3 Lys 4 (H3K4me3) deposition in embryonic stem cells. Moreover, Cfp1 is an essential component of the SETD1 histone H3K4 methyltransferase complex and functions as a critical regulator of histone methylation, cytosine methylation, cellular differentiation, and vertebrate development. Cfp1 contains a plant homeodomain (PHD) finger, a CXXC domain, and a CpG binding protein zinc finger C-terminal domain. Its CXXC domain selectively binds to non-methylated CpG islands, following by a preference for a guanosine nucleotide.


Pssm-ID: 277028  Cd Length: 46  Bit Score: 41.21  E-value: 6.83e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462511422  863 CICGLYKDEGLMIQCDKCMVWQHCDCMGVNSD----VEHYLCEQC 903
Cdd:cd15553      2 CICRSSDISRFMIGCDNCEEWYHGDCINITEKeakaIKEWYCQQC 46
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 747-807 7.40e-05

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99931  Cd Length: 102  Bit Score: 43.04  E-value: 7.40e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462511422  747 LNLPpkkknaDYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPV 807
Cdd:cd05499     33 LNIP------NYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDV 87
PHD_Ecm5p_Lid2p_like cd15518
PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), ...
 863-903 9.78e-05

PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins; The family includes Saccharomyces cerevisiae Ecm5p, Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins. Ecm5p is a JmjC domain-containing protein that directly removes histone lysine methylation via a hydroxylation reaction. It associates with the yeast Snt2p and Rpd3 deacetylase, which may play a role in regulating transcription in response to oxidative stress. Ecm5p promotes oxidative stress tolerance, while Snt2p ultimately decreases tolerance. Ecm5p contains an N-terminal ARID domain, a JmjC domain, and a C-terminal plant homeodomain (PHD) finger. Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model includes the second PHD finger of Lid2p.


Pssm-ID: 276993  Cd Length: 45  Bit Score: 40.80  E-value: 9.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462511422  863 CICGLYkDEGLMIQCDKCMVWQHCDCMG----VNSDVEHYLCEQC 903
Cdd:cd15518      2 CFCRQG-EGGTMIECEICKEWYHVKCIKngrwKLDDDDKFVCPIC 45
PHD_SHPRH cd15547
PHD finger found in E3 ubiquitin-protein ligase SHPRH; SHPRH, also termed SNF2, histone-linker, ...
 863-903 1.02e-04

PHD finger found in E3 ubiquitin-protein ligase SHPRH; SHPRH, also termed SNF2, histone-linker, PHD and RING finger domain-containing helicase, belongs to the SWI2/SNF2 family of ATP-dependent chromatin remodeling enzymes, containing the Cys3HisCys4 RING-finger characteristic of E3 ubiquitin ligases. It plays a key role in the error-free branch of DNA damage tolerance. As functional homologs of Saccharomyces cerevisiae Rad5, SHPRH and its closely-related protein, helicase like transcription factor (HLTF), act as ubiquitin ligases that cooperatively mediate Ubc13-Mms2-dependent polyubiquitination of proliferating cell nuclear antigen (PCNA) and maintain genomic stability. SHPRH contains a SNF2 domain, a H1.5 (linker histone H1 and H5) domain, a plant homeodomain (PHD) finger, a Cys3HisCys4 RING-finger, and a C-terminal helicase domain.


Pssm-ID: 277022 [Multi-domain]  Cd Length: 47  Bit Score: 40.86  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462511422  863 CICG-LYKDEG-LMIQCDKCMVWQHCDCMGVNSD---VEHYLCEQC 903
Cdd:cd15547      2 CICGeLDEIDNkHRVQCLKCGLWQHAECVNYDEEsdkREPYLCPHC 47
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
 863-903 1.15e-04

PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, Dido2, and Dido3; PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. This family also includes Dido gene encoding three alternative splicing variants (Dido1, 2, and 3), which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1 is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved PHD finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine4 (H3K4me3). Gene Dido1 is a Bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform and is ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but is involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, a SPOC module, and a long C-terminal region (CT) of unknown homology.


Pssm-ID: 277027  Cd Length: 50  Bit Score: 40.85  E-value: 1.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462511422  863 CICGLYKDEGLMIQCDKCMVWQHCDCMGVN--------SDVEHYLCEQC 903
Cdd:cd15552      2 CICRKPHNNRFMICCDRCEEWFHGDCVGITeaqgkemeENIEEYVCPKC 50
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
 493-550 1.50e-04

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) and similar proteins; KMT5C (also termed lysine N-methyltransferase 5C, lysine-specific methyltransferase 5C, suppressor of variegation 4-20 homolog 2, Su(var)4-20 homolog 2 or Suv4-20h2) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380962  Cd Length: 142  Bit Score: 43.11  E-value: 1.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462511422  493 ARFINHSCDPNCEMQKWSVNgvyRIGLYALKDMPAGTELTYDYNfHSFNVEKQQLCKC 550
Cdd:cd19185     77 AAFINHDCKPNCKFVPADGN---AACVKVLRDIEPGDEVTCFYG-EGFFGEKNEHCEC 130
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 864-903 2.12e-04

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


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 40.22  E-value: 2.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462511422  864 ICGL--YKDEGLMIQCDKCMVWQHCDCMGVNS----DVEHYLCEQC 903
Cdd:cd15517      4 ICNLetAAVDELWVQCDGCDKWFHQFCLGLSNeryaDEDKFKCPNC 49
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
 863-903 3.32e-04

PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers.


Pssm-ID: 277035  Cd Length: 47  Bit Score: 39.64  E-value: 3.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462511422  863 CICGL-YKDEGLMIQCDKCMVWQHCDCMGVNSD----VEHYLCEQC 903
Cdd:cd15560      2 CICRTpYDESQFYIGCDRCQDWFHGRCVGILQSeaekIDEYVCPQC 47
PHD_SPP1 cd16039
PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS ...
 863-903 3.33e-04

PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS component Spp1, or Complex proteins associated with set1 protein Spp1, or Suppressor of PRP protein 1, is a component of the COMPASS complex that links histone methylation to initiation of meiotic recombination. It induces double-strand break (DSB) formation by tethering to recombinationally cold regions. SPP1 interacts with H3K4me3 and Mer2, a protein required for DSB formation, to promote recruitment of potential meiotic DSB sites to the chromosomal axis. SPP1 contains a PHD finger, a zinc binding motif.


Pssm-ID: 277186  Cd Length: 46  Bit Score: 39.38  E-value: 3.33e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462511422  863 CICGLYKDEGLMIQCDKCMVWQHCDCMGVNSD----VEHYLCEQC 903
Cdd:cd16039      2 CICQKPDDGRWMIACDGCDEWYHFTCVNIPEAdvelVDSFFCPPC 46
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 739-807 3.53e-04

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 41.27  E-value: 3.53e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462511422  739 RQALAAPLLNLPpkkknaDYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPV 807
Cdd:cd05495     26 RQPVDPKLLGIP------DYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRV 88
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 497-550 3.77e-04

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.


Pssm-ID: 380980 [Multi-domain]  Cd Length: 210  Bit Score: 43.12  E-value: 3.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462511422  497 NHSCDPNCEMqkwSVNGvYRIGLYALKDMPAGTELTYDY--NFHSFNVEKQQL-------CKC 550
Cdd:cd19203    147 NHSCDPNCVI---VFNG-PHLLLRAIREIEVGEELTISYidMLMPSEERRKQLrdqycfeCDC 205
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
 864-903 4.02e-04

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


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 39.19  E-value: 4.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462511422  864 ICGLYKDEGLMIQCDKCMVWQHCDCMGVNS---DVEHYLCEQC 903
Cdd:cd15522      4 ICKKPDDGSPMIGCDECDDWYHWECVGITDeppEEDDWFCPKC 46
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 757-815 4.54e-04

Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99944  Cd Length: 98  Bit Score: 40.85  E-value: 4.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462511422  757 DYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRDVCRLR 815
Cdd:cd05512     33 DYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDTIFYRAAVRLR 91
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 720-810 5.91e-04

Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99952  Cd Length: 106  Bit Score: 40.38  E-value: 5.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511422  720 LAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTgyYKTVEAFDADMLKVFRNAEK 799
Cdd:cd05521      2 LSKKLKPLYDGIYTLKEENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNARL 79

                           90
                   ....*....|.
gi 2462511422  800 YYGRKSPVGRD 810
Cdd:cd05521     80 YNTKGSVIYKY 90
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 748-801 1.73e-03

Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99933  Cd Length: 102  Bit Score: 38.95  E-value: 1.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  748 NLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYY 801
Cdd:cd05501     23 FISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFY 76
PHD_KDM7 cd15640
PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC ...
 863-905 1.79e-03

PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. KDM7 contains a plant homeodomain (PHD) that binds Lys4-trimethylated histone 3 (H3K4me3) and a jumonji domain that demethylates either H3K9me2 or H3K27me2.


Pssm-ID: 277110  Cd Length: 50  Bit Score: 37.66  E-value: 1.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462511422  863 CICGL-YKDEGLMIQCDKCMVWQHCDCMGVN----SDVEHYLCEQCDP 905
Cdd:cd15640      2 CVCRQpYDVNRFMIECDICKDWFHGSCVQVEehhaADIDLYHCPNCEV 49
PHD_DIDO1_like cd15639
PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family ...
 859-903 2.07e-03

PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family includes three alternative splicing variants (Dido1, 2, and 3) encoded by the Dido gene, which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1, also termed DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved plant homeodomain (PHD) finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). Gene Dido is a Bonemorphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, aspen paralog and ortholog (SPOC) module, and a long C-terminal region (CT) of unknown homology. Its PHD finger interacts with H3K4me3.


Pssm-ID: 277109  Cd Length: 54  Bit Score: 37.64  E-value: 2.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462511422  859 DVIRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNS--------DVEHYLCEQC 903
Cdd:cd15639      2 NALYCICRQPHNNRFMICCDRCEEWFHGDCVGITEargrllerNGEDYICPNC 54
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
 739-802 2.69e-03

Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99940  Cd Length: 99  Bit Score: 38.52  E-value: 2.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462511422  739 RQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYG 802
Cdd:cd05508     16 KQPGAEPFLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYNG 79
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 739-811 4.50e-03

Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99929  Cd Length: 107  Bit Score: 38.17  E-value: 4.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462511422  739 RQALAAPLLNLPpkkknaDYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYygrkSPVGRDV 811
Cdd:cd05497     27 QQPVDAVKLNLP------DYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIY----NKPGDDV 89
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 495-546 6.75e-03

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


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 39.59  E-value: 6.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462511422  495 FINHSCDPNCEmqKWSVNGVyrIGLYALKDMPAGTELTYDYNFHSFNVEKQQ 546
Cdd:cd10536    153 LLNHSCDPNTI--RSFYGNT--IVVRATRPIKKGEEITICYGPHFSRMKRSE 200
 
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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