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Conserved domains on  [gi|568999701|ref|XP_006524051|]
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histone-lysine N-methyltransferase PRDM9 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
244-372 5.87e-80

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


:

Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 253.31  E-value: 5.87e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYV 323
Cdd:cd19193    2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 324 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGIK 372
Cdd:cd19193   81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
KRAB super family cl42959
krueppel associated box;
32-89 7.26e-13

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 63.77  E-value: 7.26e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568999701    32 FKDISIYFSKEEWAEMGEWEKIRYRNV-KRNYKMLISIGLRAPRPAFMCYQRQAMKPQI 89
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQKNLYRDVmLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
175-205 1.53e-12

SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localize to this region.


:

Pssm-ID: 430657  Cd Length: 31  Bit Score: 62.02  E-value: 1.53e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568999701  175 LRKKNVEVKMYRLRERKGLAYEEVSEPQDDD 205
Cdd:pfam09514   1 LRRKEVEVWMYRLRERKGVVYEEISDPQEDD 31
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
539-844 1.72e-09

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 539 KPYVCRECGRGFTQNSHLIQHQRTHTGEKPYVCRECGRGFTQK--SDLIKHQRTHTGEKPYvcRECGRGFTQKSDLIKHQ 616
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSD--LNSKSLPLSNSKASSSS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 617 RTHTGEKPYV---CRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRGF--TQKSVLIKHQRTHTgekpyvcRECGRGFT 691
Cdd:COG5048  110 LSSSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPAN-------SLSKDPSS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 692 AKSVLIQHQRTHTGEKPYVCRECGRgFTAKSNLIQHQRTHTGEKPYVCRECGRGFTAKSVLIQHQRTHTGEKPYVCRECG 771
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESP 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 772 RGFTAKSVLIQHQRTHTGE-------KPYVCRECGRGFTQKSNLIKHQRT--HTGE--KPYVCRE--CGWGFTQKSDLIQ 838
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                 ....*.
gi 568999701 839 HQRTHT 844
Cdd:COG5048  342 HILLHT 347
 
Name Accession Description Interval E-value
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
244-372 5.87e-80

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 253.31  E-value: 5.87e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYV 323
Cdd:cd19193    2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 324 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGIK 372
Cdd:cd19193   81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
KRAB smart00349
krueppel associated box;
32-89 7.26e-13

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 63.77  E-value: 7.26e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568999701    32 FKDISIYFSKEEWAEMGEWEKIRYRNV-KRNYKMLISIGLRAPRPAFMCYQRQAMKPQI 89
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQKNLYRDVmLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
175-205 1.53e-12

SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localize to this region.


Pssm-ID: 430657  Cd Length: 31  Bit Score: 62.02  E-value: 1.53e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568999701  175 LRKKNVEVKMYRLRERKGLAYEEVSEPQDDD 205
Cdd:pfam09514   1 LRRKEVEVWMYRLRERKGVVYEEISDPQEDD 31
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
539-844 1.72e-09

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 539 KPYVCRECGRGFTQNSHLIQHQRTHTGEKPYVCRECGRGFTQK--SDLIKHQRTHTGEKPYvcRECGRGFTQKSDLIKHQ 616
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSD--LNSKSLPLSNSKASSSS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 617 RTHTGEKPYV---CRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRGF--TQKSVLIKHQRTHTgekpyvcRECGRGFT 691
Cdd:COG5048  110 LSSSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPAN-------SLSKDPSS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 692 AKSVLIQHQRTHTGEKPYVCRECGRgFTAKSNLIQHQRTHTGEKPYVCRECGRGFTAKSVLIQHQRTHTGEKPYVCRECG 771
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESP 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 772 RGFTAKSVLIQHQRTHTGE-------KPYVCRECGRGFTQKSNLIKHQRT--HTGE--KPYVCRE--CGWGFTQKSDLIQ 838
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                 ....*.
gi 568999701 839 HQRTHT 844
Cdd:COG5048  342 HILLHT 347
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
32-68 1.05e-08

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 51.40  E-value: 1.05e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568999701  32 FKDISIYFSKEEWAEMGEWEKIRYRNVKR-NYKMLISI 68
Cdd:cd07765    3 FEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLVSL 40
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
250-368 1.96e-08

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: 53.49  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701   250 LRISPSgiPEAGLGVWneAS-DLPVGLHFGPYEGQITEDEEAANSG--YSWLITKGRNCYE-----YVDGQdeSQANWMR 321
Cdd:smart00317   3 LEVFKS--PGKGWGVR--ATeDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFYLFDidsdlCIDAR--RKGNLAR 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568999701   322 YVNCARDDEEQNLVAFQ-YHRKIFYRTCRVIRPGCELLVWYGDEYGQE 368
Cdd:smart00317  77 FINHSCEPNCELLFVEVnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
32-69 1.68e-07

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 48.24  E-value: 1.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568999701   32 FKDISIYFSKEEWAEMGEWEKIRYRNV-KRNYKMLISIG 69
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQRNLYRDVmLENYRNLVSLG 42
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
302-362 1.62e-04

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: 41.74  E-value: 1.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568999701  302 GRNCYEYVDGQDESQANWMRYVNcaRDDEEQNLVAFQY---HRKIFYRTCRVIRPGCELLVWYG 362
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFIN--HSCDPNCEVRVVYvngGPRIVIFALRDIKPGEELTIDYG 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-580 1.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.70e-04
                          10        20
                  ....*....|....*....|....*.
gi 568999701  555 HLIQHQRTHTGEKPYVCRECGRGFTQ 580
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
763-811 1.03e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.69  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 763 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTQKSNLIKH 811
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
244-372 5.87e-80

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 253.31  E-value: 5.87e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYV 323
Cdd:cd19193    2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 324 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGIK 372
Cdd:cd19193   81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
246-362 4.71e-33

PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family of proteins is defined based on the conserved N-terminal PR domain, which is closely related to the Su(var)3-9, enhancer of zeste, and trithorax (SET) domains of histone methyltransferases, and is specifically called PR-SET domain. The family consists of 17 members in primates. PRDMs play diverse roles in cell-cycle regulation, differentiation, and meiotic recombination. The family also contains zinc finger protein ZFPM1 and ZFPM2. ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380932  Cd Length: 83  Bit Score: 122.31  E-value: 4.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 246 LPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQItedeeaansgyswlitkgrncyeyvdgqdesqaNWMRYVNC 325
Cdd:cd10534    1 LPAGLELVLSSIPEGGLGVFARR-TIPAGTRFGPLEGVV---------------------------------NWMRFVRP 46
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568999701 326 ARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYG 362
Cdd:cd10534   47 ARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWYS 83
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
245-369 8.98e-33

PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 (also termed BLIMP-1, beta-interferon gene positive regulatory domain I-binding factor, PR domain-containing protein 1, positive regulatory domain I-binding factor 1, PRDI-BF1, or PRDI-binding factor 1) acts as a transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs.


Pssm-ID: 380964 [Multi-domain]  Cd Length: 128  Bit Score: 123.21  E-value: 8.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 245 SLPPGLRISPSGIPEAGLGVWneASD-LPVGLHFGPYEGQI-TEDE--EAANSGYSWLITKGRNCYEYVDGQDESQANWM 320
Cdd:cd19187    2 SLPRNLTLKYSSVGREVLGVW--SSDyIPRGTRFGPLVGEIyTNDPvpKGANRKYFWRIYSNGEFYHYIDGFDPSKSNWM 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 321 RYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQEL 369
Cdd:cd19187   80 RYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
244-369 1.67e-32

PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 (also termed PR domain-containing protein 11) may be involved in transcription regulation.


Pssm-ID: 380972  Cd Length: 127  Bit Score: 122.27  E-value: 1.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRISPSGIPEAGLGVWNEAsdLPVGLHFGPYEGQITEDEEAANSgYSWLITKGRNCYEYVDGQDESQANWMRYV 323
Cdd:cd19195    3 LTAPQGIEVVKDTSGESDVRCVDEV--IPKGHIFGPYEGQICTQDKSSGF-FSWLIVDKNNRYKSIDGSDETKANWMRYV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568999701 324 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQEL 369
Cdd:cd19195   80 VISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRL 125
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
246-371 1.85e-31

PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 (also termed PR domain-containing protein 12) acts as a transcription factor that is involved in the positive regulation of histone H3-K9 dimethylation.


Pssm-ID: 380973 [Multi-domain]  Cd Length: 130  Bit Score: 119.38  E-value: 1.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 246 LPPGLRISPSGIPEAGLGVWneASD-LPVGLHFGPYEGQI---TEDEEAANSGYSW--LITKGRNCYeYVDGQDESQANW 319
Cdd:cd19196    1 LPSQVIIAQSSIPGAGLGVF--SKTwIKEGTEMGPYTGRIvspEDVDPCKNNNLMWevFNEDGTVSH-FIDASQENHRSW 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568999701 320 MRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGI 371
Cdd:cd19196   78 MTFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTFLGI 129
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
246-364 1.79e-29

PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 (also termed GATA-3-binding protein G3B, lysine N-methyltransferase 8, MTB-or MTE-binding protein, PR domain-containing protein 2, retinoblastoma protein-interacting zinc finger protein, or zinc finger protein RIZ) is S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. It may function as a DNA-binding transcription factor.


Pssm-ID: 380965  Cd Length: 123  Bit Score: 113.31  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 246 LPPGLRISPSGIPEAGLGVWNEASdLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYVNC 325
Cdd:cd19188    4 LPEELELKPSAVDKTRIGVWAKKS-IPKGRKFGPFVGEKKKRSQVKNNVYMWEIYGPKRGWMCVDASDPTKGNWLRYVNW 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568999701 326 ARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDE 364
Cdd:cd19188   83 ARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWYNGE 121
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
244-371 1.95e-29

PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 (also termed PR domain-containing protein 14) acts as a transcription factor that has both positive and negative roles on transcription. It acts on regulating epigenetic modifications in the cells, playing a key role in the regulation of cell pluripotency, epigenetic reprogramming, differentiation and development. Aberrant PRDM14 expression is associated with tumorigenesis, cell migration and cell chemotherapeutic drugs resistance.


Pssm-ID: 380975  Cd Length: 133  Bit Score: 113.65  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRI---SPSGIPEAGLGVwneASDLPVGLHFGPYEG---QITEDEEAANSGYSWLITKGRNCYEYVDGQDESqA 317
Cdd:cd19198    1 LDLPEGLRVlqtSFGGTPHYGVFC---KKTIPKGTRFGPFRGrvvNTSEIKTYDDNSFMWEIFEDGKLSHFIDGRGST-G 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568999701 318 NWMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGI 371
Cdd:cd19198   77 NWMSYVNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVWYGDCYLQFMGI 130
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
246-367 4.85e-28

PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 (also termed PR domain-containing protein 6) is a putative histone-lysine N-methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. It may specifically methylate 'Lys-20' of histone H4 when associated with other proteins and in vitro.


Pssm-ID: 380968  Cd Length: 128  Bit Score: 109.49  E-value: 4.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 246 LPPGLRISPSGIPEAGLGVWnEASDLPVGLHFGPYEGQITEDEE----AANSGYSWLI--TKGRNCYeYVDGQDESQANW 319
Cdd:cd19191    1 LPDEVCLCTSSIPGLGYGIC-AAQRIPQGTWIGPFEGVLVSPEKqigaVRNTQHLWEIydQEGTLQH-FIDGGDPSKSSW 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568999701 320 MRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQ 367
Cdd:cd19191   79 MRYIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLVWYDDSYTS 126
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
243-368 1.88e-23

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus protein and similar proteins; PRDM16 (also termed PR domain-containing protein 16, transcription factor MEL1, or MDS1/EVI1-like gene 1) functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells. It is closely related to paralog of PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) which is a nuclear transcription factor essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). PRDM3 and PRDM16 are both directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380977  Cd Length: 135  Bit Score: 96.67  E-value: 1.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 243 VLSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGqiTEDEEAANSGYSW-LITKGRNCYEYVDGQDESQANWMR 321
Cdd:cd19200    7 DIPIPPDFELRESAAVGAGLGVWTKV-RIEVGEKFGPFVG--VQRSSVKDPTYAWeIVDEFGKVKFWIDASEPGTGNWMK 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568999701 322 YVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDE-YGQE 368
Cdd:cd19200   84 YIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAvYPHE 131
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
244-370 3.71e-21

PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 (also termed PR domain-containing protein 4, or PFM1) may function as a transcription factor involved in cell differentiation.


Pssm-ID: 380966  Cd Length: 133  Bit Score: 90.22  E-value: 3.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRISPSgIPEAGLGVWNEASdLPVGLHFGPYEGQIT-----EDEEAANSGYSWLITKGRNCYEYVDGQDESQAN 318
Cdd:cd19189    4 LSLPRQLYLRQS-ETGAEVGVWTKET-IPVRTCFGPLIGQQShsaevADWTDKAAPHIWKIYHNDVLEFCIITTDENECN 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568999701 319 WMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELG 370
Cdd:cd19189   82 WMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQLG 133
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
245-370 5.86e-20

PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 (also termed PR domain-containing protein 10, or tristanin) may be involved in transcriptional regulation.


Pssm-ID: 380971  Cd Length: 128  Bit Score: 86.64  E-value: 5.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 245 SLPPGLRISPSGipEAGLGVWNEASdLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYE-YVDGQDESQANWMRYV 323
Cdd:cd19194    5 SLPLILQIFRFG--ETLGGVFAKRR-IPKRTQFGPLEGPLVKKSELKDNKIHPLELEEDDGEDlYFDLSDENKCNWMMFV 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568999701 324 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELG 370
Cdd:cd19194   82 RPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
244-365 1.17e-19

PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 (also termed PR domain-containing protein 15, or zinc finger protein 298 (ZNF298)) may be involved in transcriptional regulation. It plays an essential role as a chromatin factor that modulates the transcription of upstream regulators of WNT and MAPK-ERK signaling to safeguard naive pluripotency.


Pssm-ID: 380976  Cd Length: 126  Bit Score: 85.54  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRISPsgIPEAGLGVWnEASDLPVGLHFGPYEGQITE--DEEAANSGYswLITKGRNCYeYVDGQDESQANWMR 321
Cdd:cd19199    5 SSLPDNLEIRQ--LEDGSEGVF-ALVPLVKRTQFGPFEAKRVArlDGFAVFPLK--VFEKDGSVV-YLDTSNEDDCNWMM 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568999701 322 YVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEY 365
Cdd:cd19199   79 FVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFY 122
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
245-364 1.68e-18

PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 (also termed zinc finger protein 408 (ZNF408)) may be involved in transcriptional regulation.


Pssm-ID: 380918  Cd Length: 121  Bit Score: 82.08  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 245 SLPPGLRISPSGIPEAGLGVWNEASDLPVGLHFGPYEGqitedeEAANSGyswlITKGRNCYEYVDGQD------ESQAN 318
Cdd:cd10520    4 SLPPGLALGPSLAQEERLGVWCVGDALQKGTFLGPLEE------ELESHD----LTEGGSPRQEESGQSgdvlacEQSSK 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568999701 319 WMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDE 364
Cdd:cd10520   74 WMRFACRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLWPEEN 119
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
252-364 1.72e-16

PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 (also termed PR domain-containing protein 8) may function as histone methyltransferase, preferentially acting on 'Lys-9' of histone H3.


Pssm-ID: 380969  Cd Length: 131  Bit Score: 76.70  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 252 ISPSGIPEAGL---------GVWNeASDLPVGLHFGPYEGQITEDEEAANSGyswLITKGRNCYEYVDGQDESQAN---- 318
Cdd:cd19192    1 MSHRSLWRGGSksvltdiftSVVT-TTDIPAGTIFGPCVLSFTLGYDIADIA---LKTTDKRVVPYIFRVDTGACNgsse 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568999701 319 ---WMRYVNCARDDEEQNLVAFQY-HRKIFYRTCRVIRPGCELLVWYGDE 364
Cdd:cd19192   77 psdWLRLVQPARDRHEQNLEAFRKnEGQVYFRTLRRIRKGEELLVWYSDE 126
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
244-361 2.74e-15

PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380978  Cd Length: 122  Bit Score: 72.76  E-value: 2.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLR-ISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEaaNSGYSWLITK-GRNCYEYVDGQDESQANWMR 321
Cdd:cd19201    1 LSLPGELElRKPSQDAGRSGGVWAKQ-PLPEGTRFGPYPGKLVKEPL--DPSYEWKVEAqGSKGGEGLLLLTEDSGTWLK 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568999701 322 YVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWY 361
Cdd:cd19201   78 LVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVL 117
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
246-363 3.57e-15

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, also termed PR domain-containing protein 16, or transcription factor MEL1, or MDS1/EVI1-like gene 1, functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells and is closely related to paralog of PRDM3, both of which are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380990  Cd Length: 162  Bit Score: 73.76  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 246 LPPGLRISPSGIPEAGLGVWNEaSDLPVGLHFGPYEG--------------QITED-EEAANSGYSWLITKGRNCYEY-V 309
Cdd:cd19213   20 IPSDFELRESSIPGAGLGVWAK-RKIEAGERFGPYTGvqrstlkdtnfgweQILNDvEVSSQEGCITKIVDDLGNEKFcV 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568999701 310 DGQDESQANWMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGD 363
Cdd:cd19213   99 DAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVKD 152
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
244-368 7.69e-14

PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) is a nuclear transcription factor, which is essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). It is closely related to paralog PRDM16, both o fwhich are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380991  Cd Length: 158  Bit Score: 69.97  E-value: 7.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 244 LSLPPGLRISPSGIPEAGLGVWNEASdLPVGLHFGPYEGQITEDEEAANSGYSWLITKGrNCYEYVDGQDESQANWMRYV 323
Cdd:cd19214   28 IPIPSEFELRESNIPGTGLGIWTKRK-IEVGEKFGPYVGEQRSNLKDPSYGWEVLDEFG-NVKFCIDASQPDVGSWLKYI 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568999701 324 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWY-GDEYGQE 368
Cdd:cd19214  106 RFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMkSEDYSHE 151
KRAB smart00349
krueppel associated box;
32-89 7.26e-13

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 63.77  E-value: 7.26e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568999701    32 FKDISIYFSKEEWAEMGEWEKIRYRNV-KRNYKMLISIGLRAPRPAFMCYQRQAMKPQI 89
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQKNLYRDVmLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
175-205 1.53e-12

SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localize to this region.


Pssm-ID: 430657  Cd Length: 31  Bit Score: 62.02  E-value: 1.53e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568999701  175 LRKKNVEVKMYRLRERKGLAYEEVSEPQDDD 205
Cdd:pfam09514   1 LRRKEVEVWMYRLRERKGVVYEEISDPQEDD 31
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
309-362 2.71e-12

PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 (also termed PR domain-containing protein 13) may be involved in transcriptional regulation. It mediates the balance of inhibitory and excitatory neurons in somatosensory circuits.


Pssm-ID: 380974  Cd Length: 103  Bit Score: 63.68  E-value: 2.71e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568999701 309 VDGQDESQANWMRYVNCARDDEEQNLVAFQYHR--KIFYRTCRVIRPGCELLVWYG 362
Cdd:cd19197   41 VDESGSPATEWIGLVRAARNNQEQNLEAIADLPggQIFYRALRDIQPGEELTVWYS 96
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
539-844 1.72e-09

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 539 KPYVCRECGRGFTQNSHLIQHQRTHTGEKPYVCRECGRGFTQK--SDLIKHQRTHTGEKPYvcRECGRGFTQKSDLIKHQ 616
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSD--LNSKSLPLSNSKASSSS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 617 RTHTGEKPYV---CRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRGF--TQKSVLIKHQRTHTgekpyvcRECGRGFT 691
Cdd:COG5048  110 LSSSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPAN-------SLSKDPSS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 692 AKSVLIQHQRTHTGEKPYVCRECGRgFTAKSNLIQHQRTHTGEKPYVCRECGRGFTAKSVLIQHQRTHTGEKPYVCRECG 771
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESP 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 772 RGFTAKSVLIQHQRTHTGE-------KPYVCRECGRGFTQKSNLIKHQRT--HTGE--KPYVCRE--CGWGFTQKSDLIQ 838
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                 ....*.
gi 568999701 839 HQRTHT 844
Cdd:COG5048  342 HILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
389-772 3.16e-09

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.09  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 389 TEIHPCLLCSLAFSSQKFLTQHM-----EwNHRTEIFPGTSA-RINPKPGDPCSDQLQEQHVDSQNKNDKASNEVKRKSK 462
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIrshtgE-KPSQCSYSGCDKsFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 463 PRQRISTTFPSTLKEQM--RSEESKRTVEELRT----------GQTTNTEDTVKSFIASEISSIERQCGQYFSDKSNVNE 530
Cdd:COG5048  110 LSSSSSNSNDNNLLSSHslPPSSRDPQLPDLLSisnlrnnplpGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 531 HQKTHTGEKPYVCRECGRgFTQNSHLIQHQRTHTGEKPYVCRECGRGFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKS 610
Cdd:COG5048  190 SNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 611 DLIKHQRTHTGE-------KPYVCRECGRGFTQKSVLIKHQRT--HTGE--KPYVCRE--CGRGFTQKSVLIKHQRTHTG 677
Cdd:COG5048  269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 678 EKPYVCRECGRGFT-------AKSVLIQHQRTHTGEKPYVC--RECGRGFTAKSNLIQHQRTHTGEKPYVCR--ECGRGF 746
Cdd:COG5048  349 ISPAKEKLLNSSSKfspllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428
                        410       420
                 ....*....|....*....|....*.
gi 568999701 747 TAKSVLIQHQRTHTGEKPYVCRECGR 772
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKS 454
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
251-365 4.75e-09

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: 55.04  E-value: 4.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 251 RISPSGIP---EAGLGVWnEASDLPVGLHFGPYEG-QITEDEEAANS----GYSWLITKGRNCYeYVDGqdESQANWMRY 322
Cdd:cd10522    1 KVDISMIPnlsHNGLGLF-AAETIAKGEFVGEYTGeVLDRWEEDRDSvyhyDPLYPFDLNGDIL-VIDA--GKKGNLTRF 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568999701 323 VNCARDDeeqNLVAFQYHRK----IFYRTCRVIRPGCELLVWYGDEY 365
Cdd:cd10522   77 INHSDQP---NLELIVRTLKgeqhIGFVAIRDIKPGEELFISYGPKY 120
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
32-68 1.05e-08

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 51.40  E-value: 1.05e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568999701  32 FKDISIYFSKEEWAEMGEWEKIRYRNVKR-NYKMLISI 68
Cdd:cd07765    3 FEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLVSL 40
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
250-368 1.96e-08

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: 53.49  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701   250 LRISPSgiPEAGLGVWneAS-DLPVGLHFGPYEGQITEDEEAANSG--YSWLITKGRNCYE-----YVDGQdeSQANWMR 321
Cdd:smart00317   3 LEVFKS--PGKGWGVR--ATeDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFYLFDidsdlCIDAR--RKGNLAR 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568999701   322 YVNCARDDEEQNLVAFQ-YHRKIFYRTCRVIRPGCELLVWYGDEYGQE 368
Cdd:smart00317  77 FINHSCEPNCELLFVEVnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
261-363 9.45e-08

PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 (also termed PR domain-containing protein 5) is a sequence-specific DNA-binding transcription factor that represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1.


Pssm-ID: 380967  Cd Length: 127  Bit Score: 51.52  E-value: 9.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 261 GLGVWNeASDLPVGLHFGPYEGQ---ITEDEEAANSGYSWLI--TKGRNCYeYVDGQDESQANWMRYVNCARDDEEQNLV 335
Cdd:cd19190   19 GMGLYT-ARRVKKGEKFGPFAGEkrmPNELDESMDPRLMWEVrgSKGEVLY-ILDASNPRHSNWLRFVHEAPSQEQKNLA 96
                         90       100
                 ....*....|....*....|....*...
gi 568999701 336 AFQYHRKIFYRTCRVIRPGCELLVWYGD 363
Cdd:cd19190   97 AIQEGENIFYLAVDDIETDTELLIGYLD 124
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
32-69 1.68e-07

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 48.24  E-value: 1.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568999701   32 FKDISIYFSKEEWAEMGEWEKIRYRNV-KRNYKMLISIG 69
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQRNLYRDVmLENYRNLVSLG 42
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
302-362 1.62e-04

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: 41.74  E-value: 1.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568999701  302 GRNCYEYVDGQDESQANWMRYVNcaRDDEEQNLVAFQY---HRKIFYRTCRVIRPGCELLVWYG 362
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFIN--HSCDPNCEVRVVYvngGPRIVIFALRDIKPGEELTIDYG 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-580 1.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.70e-04
                          10        20
                  ....*....|....*....|....*.
gi 568999701  555 HLIQHQRTHTGEKPYVCRECGRGFTQ 580
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
793-815 2.06e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.21  E-value: 2.06e-04
                          10        20
                  ....*....|....*....|...
gi 568999701  793 YVCRECGRGFTQKSNLIKHQRTH 815
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
723-747 2.69e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.69e-04
                          10        20
                  ....*....|....*....|....*
gi 568999701  723 NLIQHQRTHTGEKPYVCRECGRGFT 747
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
780-804 3.91e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.91e-04
                          10        20
                  ....*....|....*....|....*
gi 568999701  780 LIQHQRTHTGEKPYVCRECGRGFTQ 804
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
583-608 4.15e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.15e-04
                          10        20
                  ....*....|....*....|....*.
gi 568999701  583 DLIKHQRTHTGEKPYVCRECGRGFTQ 608
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
611-636 4.15e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.15e-04
                          10        20
                  ....*....|....*....|....*.
gi 568999701  611 DLIKHQRTHTGEKPYVCRECGRGFTQ 636
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
597-619 4.34e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 4.34e-04
                          10        20
                  ....*....|....*....|...
gi 568999701  597 YVCRECGRGFTQKSDLIKHQRTH 619
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
569-591 4.34e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 4.34e-04
                          10        20
                  ....*....|....*....|...
gi 568999701  569 YVCRECGRGFTQKSDLIKHQRTH 591
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
640-664 5.30e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.30e-04
                          10        20
                  ....*....|....*....|....*
gi 568999701  640 LIKHQRTHTGEKPYVCRECGRGFTQ 664
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
527-552 6.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.39e-04
                          10        20
                  ....*....|....*....|....*.
gi 568999701  527 NVNEHQKTHTGEKPYVCRECGRGFTQ 552
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
541-563 6.82e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 6.82e-04
                          10        20
                  ....*....|....*....|...
gi 568999701  541 YVCRECGRGFTQNSHLIQHQRTH 563
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
696-719 8.58e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 8.58e-04
                          10        20
                  ....*....|....*....|....
gi 568999701  696 LIQHQRTHTGEKPYVCRECGRGFT 719
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
752-775 8.58e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 8.58e-04
                          10        20
                  ....*....|....*....|....
gi 568999701  752 LIQHQRTHTGEKPYVCRECGRGFT 775
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
763-811 1.03e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 38.69  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 763 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTQKSNLIKH 811
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
668-691 1.16e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.16e-03
                          10        20
                  ....*....|....*....|....
gi 568999701  668 LIKHQRTHTGEKPYVCRECGRGFT 691
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
PR-SET_ZFPM1 cd19215
PR-SET domain found in zinc finger protein ZFPM1 and similar proteins; ZFPM1 (also termed ...
270-359 1.68e-03

PR-SET domain found in zinc finger protein ZFPM1 and similar proteins; ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation.


Pssm-ID: 380992  Cd Length: 110  Bit Score: 38.99  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 270 DLPVGLHFGPYEGQIT----EDEEAANSGYSWLITKGRNCyeyvdgqdesqanWMRYVNCARDDEEQNLVAFQYHRKIFY 345
Cdd:cd19215   23 SLSEGLSWGPYHGSIQssasSPGQAEESPAVTLLLVDEDC-------------WLRRLPLVSTEAEANCTIYRKGDAIWC 89
                         90
                 ....*....|....
gi 568999701 346 RTCRVIRPGCELLV 359
Cdd:cd19215   90 KTTKPVPEGELLSA 103
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
821-843 1.71e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|...
gi 568999701  821 YVCRECGWGFTQKSDLIQHQRTH 843
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
679-727 1.78e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.92  E-value: 1.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 679 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTAKSNLIQH 727
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
807-832 2.36e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.36e-03
                          10        20
                  ....*....|....*....|....*.
gi 568999701  807 NLIKHQRTHTGEKPYVCRECGWGFTQ 832
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
709-731 3.18e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 3.18e-03
                          10        20
                  ....*....|....*....|...
gi 568999701  709 YVCRECGRGFTAKSNLIQHQRTH 731
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
625-647 3.51e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 3.51e-03
                          10        20
                  ....*....|....*....|...
gi 568999701  625 YVCRECGRGFTQKSVLIKHQRTH 647
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
653-675 3.51e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 3.51e-03
                          10        20
                  ....*....|....*....|...
gi 568999701  653 YVCRECGRGFTQKSVLIKHQRTH 675
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
635-708 6.30e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568999701 635 TQKSVLIKHQRTHTGE----KPYVCRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRG--FTAKSVLIQHQRTHTGEKP 708
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPS 91
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
735-783 6.36e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.38  E-value: 6.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568999701 735 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTAKSVLIQH 783
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
780-844 8.52e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 8.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568999701 780 LIQHQRTHTGE----KPYVCRECGRGFTQKSNLIKHQRTHTGEKPYVCRECGWGFTQK--SDLIQHQRTHT 844
Cdd:COG5048   17 SSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHH 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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