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Conserved domains on  [gi|1907123475|ref|XP_036016346|]
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histone-lysine N-methyltransferase PRDM9 isoform X5 [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 ...
 251-379 6.39e-81

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: 255.62  E-value: 6.39e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYV 330
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 331 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGIK 379
Cdd:cd19193    81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 186-212 7.21e-11

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: 57.39  E-value: 7.21e-11
                          10        20
                  ....*....|....*....|....*..
gi 1907123475 186 NVEVKMYRLRERKGLAYEEVSEPQDDD 212
Cdd:pfam09514   5 EVEVWMYRLRERKGVVYEEISDPQEDD 31
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
396-779 3.45e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.09  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 396 TEIHPCLLCSLAFSSQKFLTQHM-----EwNHRTEIFPGTSA-RINPKPGDPCSDQLQEQHVDSQNKNDKASNEVKRKSK 469
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIrshtgE-KPSQCSYSGCDKsFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 470 PRQRISTTFPSTLKEQM--RSEESKRTVEELRT----------GQTTNTEDTVKSFIASEISSIERQCGQYFSDKSNVNE 537
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHslPPSSRDPQLPDLLSisnlrnnplpGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 538 HQKTHTGEKPYVCRECGRgFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKS 617
Cdd:COG5048   190 SNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 618 VLIKHQRTHTGE-------KPYVCRECGRGFTQKSVLIKHQRT--HTGE--KPYVCRE--CGRGFTAKSVLIQHQRTHTG 684
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 685 EKPYVCRECGRGFTAKSNL-------IQHQRTHTGEKPYVC--RECGRGFTAKSVLIQHQRTHTGEKPYVCR--ECGRGF 753
Cdd:COG5048   349 ISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428

                         410       420
                  ....*....|....*....|....*.
gi 1907123475 754 TAKSVLIQHQRTHTGEKPYVCRECGR 779
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 772-794 1.61e-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: 1.61e-04
                          10        20
                  ....*....|....*....|...
gi 1907123475 772 YVCRECGRGFTQKSNLIKHQRTH 794
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 800-822 1.36e-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: 1.36e-03
                          10        20
                  ....*....|....*....|...
gi 1907123475 800 YVCRECGWGFTQKSDLIQHQRTH 822
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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 ...
 251-379 6.39e-81

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: 255.62  E-value: 6.39e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYV 330
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 331 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGIK 379
Cdd:cd19193    81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 186-212 7.21e-11

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: 57.39  E-value: 7.21e-11
                          10        20
                  ....*....|....*....|....*..
gi 1907123475 186 NVEVKMYRLRERKGLAYEEVSEPQDDD 212
Cdd:pfam09514   5 EVEVWMYRLRERKGVVYEEISDPQEDD 31
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
396-779 3.45e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.09  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 396 TEIHPCLLCSLAFSSQKFLTQHM-----EwNHRTEIFPGTSA-RINPKPGDPCSDQLQEQHVDSQNKNDKASNEVKRKSK 469
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIrshtgE-KPSQCSYSGCDKsFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 470 PRQRISTTFPSTLKEQM--RSEESKRTVEELRT----------GQTTNTEDTVKSFIASEISSIERQCGQYFSDKSNVNE 537
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHslPPSSRDPQLPDLLSisnlrnnplpGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 538 HQKTHTGEKPYVCRECGRgFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKS 617
Cdd:COG5048   190 SNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 618 VLIKHQRTHTGE-------KPYVCRECGRGFTQKSVLIKHQRT--HTGE--KPYVCRE--CGRGFTAKSVLIQHQRTHTG 684
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 685 EKPYVCRECGRGFTAKSNL-------IQHQRTHTGEKPYVC--RECGRGFTAKSVLIQHQRTHTGEKPYVCR--ECGRGF 753
Cdd:COG5048   349 ISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428

                         410       420
                  ....*....|....*....|....*.
gi 1907123475 754 TAKSVLIQHQRTHTGEKPYVCRECGR 779
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPLLCSILKS 454
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 257-375 8.38e-09

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: 54.26  E-value: 8.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475  257 LRISPSgiPEAGLGVWneAS-DLPVGLHFGPYEGQITEDEEAANSG--YSWLITKGRNCYE-----YVDGQdeSQANWMR 328
Cdd:smart00317   3 LEVFKS--PGKGWGVR--ATeDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFYLFDidsdlCIDAR--RKGNLAR 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907123475  329 YVNCARDDEEQNLVAFQ-YHRKIFYRTCRVIRPGCELLVWYGDEYGQE 375
Cdd:smart00317  77 FINHSCEPNCELLFVEVnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 309-369 1.13e-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: 42.51  E-value: 1.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907123475 309 GRNCYEYVDGQDESQANWMRYVNcaRDDEEQNLVAFQY---HRKIFYRTCRVIRPGCELLVWYG 369
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFIN--HSCDPNCEVRVVYvngGPRIVIFALRDIKPGEELTIDYG 115
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 772-794 1.61e-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: 1.61e-04
                          10        20
                  ....*....|....*....|...
gi 1907123475 772 YVCRECGRGFTQKSNLIKHQRTH 794
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
702-726 1.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.85e-04
                          10        20
                  ....*....|....*....|....*
gi 1907123475 702 NLIQHQRTHTGEKPYVCRECGRGFT 726
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 742-790 7.99e-04

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: 39.08  E-value: 7.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 742 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTQKSNLIKH 790
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 800-822 1.36e-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: 1.36e-03
                          10        20
                  ....*....|....*....|...
gi 1907123475 800 YVCRECGWGFTQKSDLIQHQRTH 822
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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 ...
 251-379 6.39e-81

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: 255.62  E-value: 6.39e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYV 330
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 331 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGIK 379
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 ...
 253-369 6.26e-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: 121.92  E-value: 6.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 253 LPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQItedeeaansgyswlitkgrncyeyvdgqdesqaNWMRYVNC 332
Cdd:cd10534     1 LPAGLELVLSSIPEGGLGVFARR-TIPAGTRFGPLEGVV---------------------------------NWMRFVRP 46

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907123475 333 ARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYG 369
Cdd:cd10534    47 ARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWYS 83
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 251-376 6.90e-33

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: 123.43  E-value: 6.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRISPSGIPEAGLGVWNEAsdLPVGLHFGPYEGQITEDEEAANSgYSWLITKGRNCYEYVDGQDESQANWMRYV 330
Cdd:cd19195     3 LTAPQGIEVVKDTSGESDVRCVDEV--IPKGHIFGPYEGQICTQDKSSGF-FSWLIVDKNNRYKSIDGSDETKANWMRYV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907123475 331 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQEL 376
Cdd:cd19195    80 VISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRL 125
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 252-376 8.72e-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: 8.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 252 SLPPGLRISPSGIPEAGLGVWneASD-LPVGLHFGPYEGQI-TEDE--EAANSGYSWLITKGRNCYEYVDGQDESQANWM 327
Cdd:cd19187     2 SLPRNLTLKYSSVGREVLGVW--SSDyIPRGTRFGPLVGEIyTNDPvpKGANRKYFWRIYSNGEFYHYIDGFDPSKSNWM 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 328 RYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQEL 376
Cdd:cd19187    80 RYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 253-378 1.80e-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: 1.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 253 LPPGLRISPSGIPEAGLGVWneASD-LPVGLHFGPYEGQI---TEDEEAANSGYSW--LITKGRNCYeYVDGQDESQANW 326
Cdd:cd19196     1 LPSQVIIAQSSIPGAGLGVF--SKTwIKEGTEMGPYTGRIvspEDVDPCKNNNLMWevFNEDGTVSH-FIDASQENHRSW 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907123475 327 MRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGI 378
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 ...
 253-371 4.66e-30

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: 115.23  E-value: 4.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 253 LPPGLRISPSGIPEAGLGVWNEASdLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYVNC 332
Cdd:cd19188     4 LPEELELKPSAVDKTRIGVWAKKS-IPKGRKFGPFVGEKKKRSQVKNNVYMWEIYGPKRGWMCVDASDPTKGNWLRYVNW 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907123475 333 ARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDE 371
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 ...
 251-378 1.77e-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: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRI---SPSGIPEAGLGVwneASDLPVGLHFGPYEG---QITEDEEAANSGYSWLITKGRNCYEYVDGQDESqA 324
Cdd:cd19198     1 LDLPEGLRVlqtSFGGTPHYGVFC---KKTIPKGTRFGPFRGrvvNTSEIKTYDDNSFMWEIFEDGKLSHFIDGRGST-G 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907123475 325 NWMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGI 378
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 ...
 253-374 4.12e-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: 109.87  E-value: 4.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 253 LPPGLRISPSGIPEAGLGVWnEASDLPVGLHFGPYEGQITEDEE----AANSGYSWLI--TKGRNCYeYVDGQDESQANW 326
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGIC-AAQRIPQGTWIGPFEGVLVSPEKqigaVRNTQHLWEIydQEGTLQH-FIDGGDPSKSSW 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907123475 327 MRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQ 374
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 ...
 250-375 1.81e-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: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 250 VLSLPPGLRISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGqiTEDEEAANSGYSW-LITKGRNCYEYVDGQDESQANWMR 328
Cdd:cd19200     7 DIPIPPDFELRESAAVGAGLGVWTKV-RIEVGEKFGPFVG--VQRSSVKDPTYAWeIVDEFGKVKFWIDASEPGTGNWMK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907123475 329 YVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDE-YGQE 375
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 ...
 251-377 3.24e-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: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRISPSgIPEAGLGVWNEASdLPVGLHFGPYEGQIT-----EDEEAANSGYSWLITKGRNCYEYVDGQDESQAN 325
Cdd:cd19189     4 LSLPRQLYLRQS-ETGAEVGVWTKET-IPVRTCFGPLIGQQShsaevADWTDKAAPHIWKIYHNDVLEFCIITTDENECN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907123475 326 WMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELG 377
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 ...
 252-377 3.19e-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: 87.02  E-value: 3.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 252 SLPPGLRISPSGipEAGLGVWNEASdLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYE-YVDGQDESQANWMRYV 330
Cdd:cd19194     5 SLPLILQIFRFG--ETLGGVFAKRR-IPKRTQFGPLEGPLVKKSELKDNKIHPLELEEDDGEDlYFDLSDENKCNWMMFV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907123475 331 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELG 377
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 ...
 251-372 1.14e-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: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRISPsgIPEAGLGVWnEASDLPVGLHFGPYEGQITE--DEEAANSGYswLITKGRNCYeYVDGQDESQANWMR 328
Cdd:cd19199     5 SSLPDNLEIRQ--LEDGSEGVF-ALVPLVKRTQFGPFEAKRVArlDGFAVFPLK--VFEKDGSVV-YLDTSNEDDCNWMM 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907123475 329 YVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEY 372
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 ...
 252-371 3.46e-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: 81.31  E-value: 3.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 252 SLPPGLRISPSGIPEAGLGVWNEASDLPVGLHFGPYEGQITedeeaansgySWLITKGRNCYEYVDGQD------ESQAN 325
Cdd:cd10520     4 SLPPGLALGPSLAQEERLGVWCVGDALQKGTFLGPLEEELE----------SHDLTEGGSPRQEESGQSgdvlacEQSSK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907123475 326 WMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDE 371
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 ...
 259-371 1.68e-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: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 259 ISPSGIPEAGL---------GVWNeASDLPVGLHFGPYEGQITEDEEAANSGyswLITKGRNCYEYVDGQDESQAN---- 325
Cdd:cd19192     1 MSHRSLWRGGSksvltdiftSVVT-TTDIPAGTIFGPCVLSFTLGYDIADIA---LKTTDKRVVPYIFRVDTGACNgsse 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907123475 326 ---WMRYVNCARDDEEQNLVAFQY-HRKIFYRTCRVIRPGCELLVWYGDE 371
Cdd:cd19192    77 psdWLRLVQPARDRHEQNLEAFRKnEGQVYFRTLRRIRKGEELLVWYSDE 126
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 251-368 2.47e-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: 73.15  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLR-ISPSGIPEAGLGVWNEAsDLPVGLHFGPYEGQITEDEEaaNSGYSWLITK-GRNCYEYVDGQDESQANWMR 328
Cdd:cd19201     1 LSLPGELElRKPSQDAGRSGGVWAKQ-PLPEGTRFGPYPGKLVKEPL--DPSYEWKVEAqGSKGGEGLLLLTEDSGTWLK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907123475 329 YVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWY 368
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, ...
 253-370 4.96e-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: 73.37  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 253 LPPGLRISPSGIPEAGLGVWNEaSDLPVGLHFGPYEG--------------QITED-EEAANSGYSWLITKGRNCYEY-V 316
Cdd:cd19213    20 IPSDFELRESSIPGAGLGVWAK-RKIEAGERFGPYTGvqrstlkdtnfgweQILNDvEVSSQEGCITKIVDDLGNEKFcV 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907123475 317 DGQDESQANWMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGD 370
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 ...
 251-375 8.72e-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: 69.58  E-value: 8.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 251 LSLPPGLRISPSGIPEAGLGVWNEASdLPVGLHFGPYEGQITEDEEAANSGYSWLITKGrNCYEYVDGQDESQANWMRYV 330
Cdd:cd19214    28 IPIPSEFELRESNIPGTGLGIWTKRK-IEVGEKFGPYVGEQRSNLKDPSYGWEVLDEFG-NVKFCIDASQPDVGSWLKYI 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907123475 331 NCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWY-GDEYGQE 375
Cdd:cd19214   106 RFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMkSEDYSHE 151
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 316-369 2.64e-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: 2.64e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907123475 316 VDGQDESQANWMRYVNCARDDEEQNLVAFQYHR--KIFYRTCRVIRPGCELLVWYG 369
Cdd:cd19197    41 VDESGSPATEWIGLVRAARNNQEQNLEAIADLPggQIFYRALRDIQPGEELTVWYS 96
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 186-212 7.21e-11

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: 57.39  E-value: 7.21e-11
                          10        20
                  ....*....|....*....|....*..
gi 1907123475 186 NVEVKMYRLRERKGLAYEEVSEPQDDD 212
Cdd:pfam09514   5 EVEVWMYRLRERKGVVYEEISDPQEDD 31
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
396-779 3.45e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.09  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 396 TEIHPCLLCSLAFSSQKFLTQHM-----EwNHRTEIFPGTSA-RINPKPGDPCSDQLQEQHVDSQNKNDKASNEVKRKSK 469
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIrshtgE-KPSQCSYSGCDKsFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 470 PRQRISTTFPSTLKEQM--RSEESKRTVEELRT----------GQTTNTEDTVKSFIASEISSIERQCGQYFSDKSNVNE 537
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHslPPSSRDPQLPDLLSisnlrnnplpGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 538 HQKTHTGEKPYVCRECGRgFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKS 617
Cdd:COG5048   190 SNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 618 VLIKHQRTHTGE-------KPYVCRECGRGFTQKSVLIKHQRT--HTGE--KPYVCRE--CGRGFTAKSVLIQHQRTHTG 684
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 685 EKPYVCRECGRGFTAKSNL-------IQHQRTHTGEKPYVC--RECGRGFTAKSVLIQHQRTHTGEKPYVCR--ECGRGF 753
Cdd:COG5048   349 ISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428

                         410       420
                  ....*....|....*....|....*.
gi 1907123475 754 TAKSVLIQHQRTHTGEKPYVCRECGR 779
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPLLCSILKS 454
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 258-372 4.62e-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: 4.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 258 RISPSGIP---EAGLGVWnEASDLPVGLHFGPYEG-QITEDEEAANS----GYSWLITKGRNCYeYVDGqdESQANWMRY 329
Cdd:cd10522     1 KVDISMIPnlsHNGLGLF-AAETIAKGEFVGEYTGeVLDRWEEDRDSvyhyDPLYPFDLNGDIL-VIDA--GKKGNLTRF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907123475 330 VNCARDDeeqNLVAFQYHRK----IFYRTCRVIRPGCELLVWYGDEY 372
Cdd:cd10522    77 INHSDQP---NLELIVRTLKgeqhIGFVAIRDIKPGEELFISYGPKY 120
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 257-375 8.38e-09

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: 54.26  E-value: 8.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475  257 LRISPSgiPEAGLGVWneAS-DLPVGLHFGPYEGQITEDEEAANSG--YSWLITKGRNCYE-----YVDGQdeSQANWMR 328
Cdd:smart00317   3 LEVFKS--PGKGWGVR--ATeDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFYLFDidsdlCIDAR--RKGNLAR 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907123475  329 YVNCARDDEEQNLVAFQ-YHRKIFYRTCRVIRPGCELLVWYGDEYGQE 375
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 ...
 268-370 9.19e-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: 9.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 268 GLGVWNeASDLPVGLHFGPYEGQ---ITEDEEAANSGYSWLI--TKGRNCYeYVDGQDESQANWMRYVNCARDDEEQNLV 342
Cdd:cd19190    19 GMGLYT-ARRVKKGEKFGPFAGEkrmPNELDESMDPRLMWEVrgSKGEVLY-ILDASNPRHSNWLRFVHEAPSQEQKNLA 96

                          90       100
                  ....*....|....*....|....*...
gi 1907123475 343 AFQYHRKIFYRTCRVIRPGCELLVWYGD 370
Cdd:cd19190    97 AIQEGENIFYLAVDDIETDTELLIGYLD 124
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
546-823 4.07e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 546 KPYVCRECGRGFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQK--SDLIKHQRTHTGEKPYvcRECGRGFTQKSVLIKHQ 623
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSD--LNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 624 RTHTGEKPYV---CRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRGFTA-----------------------KSVLIQ 677
Cdd:COG5048   110 LSSSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsnslhpplpanslskdpssnLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 678 HQRTHTGEKPYVCRECGRgFTAKSNLIQHQRTHTGEKPYVCRECGRGFTAKSVLIQHQRTHTGEKPYVCRECGRGFTAKS 757
Cdd:COG5048   190 SNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907123475 758 VLIQHQRTHTGE-------KPYVCRECGRGFTQKSNLIKHQRT--HTGE--KPYVCRE--CGWGFTQKSDLIQHQRTHT 823
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 309-369 1.13e-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: 42.51  E-value: 1.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907123475 309 GRNCYEYVDGQDESQANWMRYVNcaRDDEEQNLVAFQY---HRKIFYRTCRVIRPGCELLVWYG 369
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFIN--HSCDPNCEVRVVYvngGPRIVIFALRDIKPGEELTIDYG 115
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 772-794 1.61e-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: 1.61e-04
                          10        20
                  ....*....|....*....|...
gi 1907123475 772 YVCRECGRGFTQKSNLIKHQRTH 794
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
702-726 1.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.85e-04
                          10        20
                  ....*....|....*....|....*
gi 1907123475 702 NLIQHQRTHTGEKPYVCRECGRGFT 726
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
759-783 2.71e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.71e-04
                          10        20
                  ....*....|....*....|....*
gi 1907123475 759 LIQHQRTHTGEKPYVCRECGRGFTQ 783
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
562-587 2.84e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.84e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907123475 562 DLIKHQRTHTGEKPYVCRECGRGFTQ 587
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
590-615 2.84e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.84e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907123475 590 DLIKHQRTHTGEKPYVCRECGRGFTQ 615
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 576-598 3.41e-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: 38.44  E-value: 3.41e-04
                          10        20
                  ....*....|....*....|...
gi 1907123475 576 YVCRECGRGFTQKSDLIKHQRTH 598
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 548-570 3.41e-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: 38.44  E-value: 3.41e-04
                          10        20
                  ....*....|....*....|...
gi 1907123475 548 YVCRECGRGFTQKSDLIKHQRTH 570
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
619-643 3.63e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.63e-04
                          10        20
                  ....*....|....*....|....*
gi 1907123475 619 LIKHQRTHTGEKPYVCRECGRGFTQ 643
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
534-559 4.29e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.29e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907123475 534 NVNEHQKTHTGEKPYVCRECGRGFTQ 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
731-754 5.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.99e-04
                          10        20
                  ....*....|....*....|....
gi 1907123475 731 LIQHQRTHTGEKPYVCRECGRGFT 754
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
675-698 5.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.99e-04
                          10        20
                  ....*....|....*....|....
gi 1907123475 675 LIQHQRTHTGEKPYVCRECGRGFT 698
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 742-790 7.99e-04

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: 39.08  E-value: 7.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 742 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTQKSNLIKH 790
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
647-670 8.05e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 8.05e-04
                          10        20
                  ....*....|....*....|....
gi 1907123475 647 LIKHQRTHTGEKPYVCRECGRGFT 670
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 800-822 1.36e-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: 1.36e-03
                          10        20
                  ....*....|....*....|...
gi 1907123475 800 YVCRECGWGFTQKSDLIQHQRTH 822
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 658-706 1.37e-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: 38.31  E-value: 1.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 658 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTAKSNLIQH 706
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
786-811 1.63e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.63e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907123475 786 NLIKHQRTHTGEKPYVCRECGWGFTQ 811
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PR-SET_ZFPM1 cd19215
PR-SET domain found in zinc finger protein ZFPM1 and similar proteins; ZFPM1 (also termed ...
 277-366 2.45e-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: 38.22  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 277 DLPVGLHFGPYEGQIT----EDEEAANSGYSWLITKGRNCyeyvdgqdesqanWMRYVNCARDDEEQNLVAFQYHRKIFY 352
Cdd:cd19215    23 SLSEGLSWGPYHGSIQssasSPGQAEESPAVTLLLVDEDC-------------WLRRLPLVSTEAEANCTIYRKGDAIWC 89

                          90
                  ....*....|....
gi 1907123475 353 RTCRVIRPGCELLV 366
Cdd:cd19215    90 KTTKPVPEGELLSA 103
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 688-710 2.58e-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: 2.58e-03
                          10        20
                  ....*....|....*....|...
gi 1907123475 688 YVCRECGRGFTAKSNLIQHQRTH 710
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 632-654 2.79e-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: 2.79e-03
                          10        20
                  ....*....|....*....|...
gi 1907123475 632 YVCRECGRGFTQKSVLIKHQRTH 654
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 604-626 2.79e-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: 2.79e-03
                          10        20
                  ....*....|....*....|...
gi 1907123475 604 YVCRECGRGFTQKSVLIKHQRTH 626
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 714-762 4.94e-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: 36.77  E-value: 4.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907123475 714 KPYvCRECGRGFTAKSVLIQHQRTHTgekpYVCRECGRGFTAKSVLIQH 762
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
614-687 8.12e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907123475 614 TQKSVLIKHQRTHTGE----KPYVCRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRG--FTAKSVLIQHQRTHTGEKP 687
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPS 91
 
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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