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Conserved domains on  [gi|1777535687|ref|NP_001363829|]
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histone-lysine N-methyltransferase PRDM9 isoform PRDM9 B [Homo sapiens]

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 ...
 240-368 8.53e-79

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: 251.00  E-value: 8.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 240 LSLPPGLRIGPSGIPQAGLGVWNEAsDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWANWMRYV 319
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1777535687 320 NCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGIK 368
Cdd:cd19193    81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
611-878 5.16e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.42  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 611 RECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRgFSRQSVLLTHQRRHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEK 690
Cdd:COG5048   175 SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 691 PYVCRECGR------GFSWQSVLLTHQRTHTG-EKPYVCRECGRGFSNKSHLLRHQRT--HTGE--KPYVCRE--CGRGF 757
Cdd:COG5048   254 SSSASESPRsslptaSSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 758 RDKSHLLRHQRTHTGEKPYVC--RECGRGFRDKSNLLSHQRTH-----TGEKPYVC--RECGRGFSNKSHLLRHQRTHTG 828
Cdd:COG5048   334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLS 413

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1777535687 829 EKPYVCR--ECGRGFRNKSHLLRHQRTHTGEKPYVCRECGRgFSDRSSLCYH 878
Cdd:COG5048   414 FRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 171-201 4.01e-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: 58.16  E-value: 4.01e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1777535687 171 LRKKETERKMYSLRERKGHAYKEVSEPQDDD 201
Cdd:pfam09514   1 LRRKEVEVWMYRLRERKGVVYEEISDPQEDD 31
KRAB super family cl42959
krueppel associated box;
27-85 1.70e-10

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 57.22  E-value: 1.70e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687   27 AFKDISIYFTKEEWAEMGDWEKTRYRNV-KRNYNALITIGLRATRPAFMCHRRQAIKLQV 85
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVmLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
528-671 5.32e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 528 ECGQGFSVKSDVITHQRT--HTGEKL--YVCRE--CGRGFSWKSHLLIHQRIHTGEKPYVCRECGRGfSWQSVLLT---- 597
Cdd:COG5048   294 QCNISFSRSSPLTRHLRSvnHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSS-SKFSPLLNnepp 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 598 ----HQRTHTGEKPYVC--RECGRGFSRQSVLLTHQRRHTGEKPYVCR--ECGRGFSRQSVLLTHQRRHTGEKPYVCREC 669
Cdd:COG5048   373 qslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL 452


                  ..
gi 1777535687 670 GR 671
Cdd:COG5048   453 KS 454
 
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 ...
 240-368 8.53e-79

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: 251.00  E-value: 8.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 240 LSLPPGLRIGPSGIPQAGLGVWNEAsDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWANWMRYV 319
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1777535687 320 NCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGIK 368
Cdd:cd19193    81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
611-878 5.16e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.42  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 611 RECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRgFSRQSVLLTHQRRHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEK 690
Cdd:COG5048   175 SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 691 PYVCRECGR------GFSWQSVLLTHQRTHTG-EKPYVCRECGRGFSNKSHLLRHQRT--HTGE--KPYVCRE--CGRGF 757
Cdd:COG5048   254 SSSASESPRsslptaSSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 758 RDKSHLLRHQRTHTGEKPYVC--RECGRGFRDKSNLLSHQRTH-----TGEKPYVC--RECGRGFSNKSHLLRHQRTHTG 828
Cdd:COG5048   334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLS 413

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1777535687 829 EKPYVCR--ECGRGFRNKSHLLRHQRTHTGEKPYVCRECGRgFSDRSSLCYH 878
Cdd:COG5048   414 FRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 171-201 4.01e-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: 58.16  E-value: 4.01e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1777535687 171 LRKKETERKMYSLRERKGHAYKEVSEPQDDD 201
Cdd:pfam09514   1 LRRKEVEVWMYRLRERKGVVYEEISDPQEDD 31
KRAB smart00349
krueppel associated box;
27-85 1.70e-10

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 57.22  E-value: 1.70e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687   27 AFKDISIYFTKEEWAEMGDWEKTRYRNV-KRNYNALITIGLRATRPAFMCHRRQAIKLQV 85
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVmLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 246-364 2.98e-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: 53.11  E-value: 2.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687  246 LRIGPSgiPQAGLGVWneAS-DLPLGLHFGPYEGRITEDEEAANNG--YSWLITKGRNCYE-----YVDGKDKSwaNWMR 317
Cdd:smart00317   3 LEVFKS--PGKGWGVR--ATeDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFYLFDidsdlCIDARRKG--NLAR 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1777535687  318 YVNCARDDEEQNLVAFQ-YHRQIFYRTCRVIRPGCELLVWYGDEYGQE 364
Cdd:smart00317  77 FINHSCEPNCELLFVEVnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 27-62 1.99e-07

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: 47.93  E-value: 1.99e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1777535687  27 AFKDISIYFTKEEWAEMGDWEKTRYRNVKR-NYNALI 62
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
528-671 5.32e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 528 ECGQGFSVKSDVITHQRT--HTGEKL--YVCRE--CGRGFSWKSHLLIHQRIHTGEKPYVCRECGRGfSWQSVLLT---- 597
Cdd:COG5048   294 QCNISFSRSSPLTRHLRSvnHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSS-SKFSPLLNnepp 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 598 ----HQRTHTGEKPYVC--RECGRGFSRQSVLLTHQRRHTGEKPYVCR--ECGRGFSRQSVLLTHQRRHTGEKPYVCREC 669
Cdd:COG5048   373 qslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL 452


                  ..
gi 1777535687 670 GR 671
Cdd:COG5048   453 KS 454
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 28-65 2.71e-06

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: 44.77  E-value: 2.71e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1777535687  28 FKDISIYFTKEEWAEMGDWEKTRYRNV-KRNYNALITIG 65
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQRNLYRDVmLENYRNLVSLG 42
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 298-358 3.07e-05

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: 44.05  E-value: 3.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777535687 298 GRNCYEYVDGKDKSWANWMRYVNcaRDDEEQNLVAFQY---HRQIFYRTCRVIRPGCELLVWYG 358
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFIN--HSCDPNCEVRVVYvngGPRIVIFALRDIKPGEELTIDYG 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
818-843 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 1777535687 818 HLLRHQRTHTGEKPYVCRECGRGFRN 843
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
595-619 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|....*
gi 1777535687 595 LLTHQRTHTGEKPYVCRECGRGFSR 619
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
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 ...
 240-368 8.53e-79

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: 251.00  E-value: 8.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 240 LSLPPGLRIGPSGIPQAGLGVWNEAsDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWANWMRYV 319
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEA-PIPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1777535687 320 NCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGIK 368
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 ...
 242-358 6.55e-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: 6.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 242 LPPGLRIGPSGIPQAGLGVWNEAsDLPLGLHFGPYEGRItedeeaanngyswlitkgrncyeyvdgkdkswaNWMRYVNC 321
Cdd:cd10534     1 LPAGLELVLSSIPEGGLGVFARR-TIPAGTRFGPLEGVV---------------------------------NWMRFVRP 46

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1777535687 322 ARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYG 358
Cdd:cd10534    47 ARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWYS 83
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 242-367 6.74e-33

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: 123.62  E-value: 6.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 242 LPPGLRIGPSGIPQAGLGVWneASD-LPLGLHFGPYEGRI---TEDEEAANNGYSW--LITKGRNCYeYVDGKDKSWANW 315
Cdd:cd19196     1 LPSQVIIAQSSIPGAGLGVF--SKTwIKEGTEMGPYTGRIvspEDVDPCKNNNLMWevFNEDGTVSH-FIDASQENHRSW 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1777535687 316 MRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGI 367
Cdd:cd19196    78 MTFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTFLGI 129
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 240-367 3.87e-32

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: 121.35  E-value: 3.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 240 LSLPPGLRI---GPSGIPQAGLGVwneASDLPLGLHFGPYEGRI---TEDEEAANNGYSWLITKGRNCYEYVDGKDKSwA 313
Cdd:cd19198     1 LDLPEGLRVlqtSFGGTPHYGVFC---KKTIPKGTRFGPFRGRVvntSEIKTYDDNSFMWEIFEDGKLSHFIDGRGST-G 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1777535687 314 NWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGI 367
Cdd:cd19198    77 NWMSYVNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVWYGDCYLQFMGI 130
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 238-365 1.13e-30

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: 117.27  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 238 SALSLPPGLRIGPSGIPQAGLGVWNEAsdLPLGLHFGPYEGRITEDEEAANNgYSWLITKGRNCYEYVDGKDKSWANWMR 317
Cdd:cd19195     1 AALTAPQGIEVVKDTSGESDVRCVDEV--IPKGHIFGPYEGQICTQDKSSGF-FSWLIVDKNNRYKSIDGSDETKANWMR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1777535687 318 YVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQEL 365
Cdd:cd19195    78 YVVISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRL 125
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 241-365 2.27e-30

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: 116.27  E-value: 2.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 241 SLPPGLRIGPSGIPQAGLGVWneASD-LPLGLHFGPYEGRI-TEDE--EAANNGYSWLITKGRNCYEYVDGKDKSWANWM 316
Cdd:cd19187     2 SLPRNLTLKYSSVGREVLGVW--SSDyIPRGTRFGPLVGEIyTNDPvpKGANRKYFWRIYSNGEFYHYIDGFDPSKSNWM 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1777535687 317 RYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQEL 365
Cdd:cd19187    80 RYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 242-360 3.82e-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: 112.53  E-value: 3.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 242 LPPGLRIGPSGIPQAGLGVWNEASdLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWANWMRYVNC 321
Cdd:cd19188     4 LPEELELKPSAVDKTRIGVWAKKS-IPKGRKFGPFVGEKKKRSQVKNNVYMWEIYGPKRGWMCVDASDPTKGNWLRYVNW 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1777535687 322 ARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDE 360
Cdd:cd19188    83 ARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWYNGE 121
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 242-363 1.31e-25

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: 102.55  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 242 LPPGLRIGPSGIPQAGLGVWnEASDLPLGLHFGPYEG-RITEDEEAA---NNGYSWLI--TKGRNCYeYVDGKDKSWANW 315
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGIC-AAQRIPQGTWIGPFEGvLVSPEKQIGavrNTQHLWEIydQEGTLQH-FIDGGDPSKSSW 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1777535687 316 MRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQ 363
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 ...
 240-364 2.32e-22

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: 93.59  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 240 LSLPPGLRIGPSGIPQAGLGVWNEAsDLPLGLHFGPYEGriTEDEEAANNGYSW-LITKGRNCYEYVDGKDKSWANWMRY 318
Cdd:cd19200     8 IPIPPDFELRESAAVGAGLGVWTKV-RIEVGEKFGPFVG--VQRSSVKDPTYAWeIVDEFGKVKFWIDASEPGTGNWMKY 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1777535687 319 VNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDE-YGQE 364
Cdd:cd19200    85 IRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAvYPHE 131
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 237-366 2.95e-18

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: 81.74  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 237 RSALSLPPGLRIGPSgIPQAGLGVWNEASdLPLGLHFGPYEGRIT-----EDEEAANNGYSWLITKGRNCYEYVDGKDKS 311
Cdd:cd19189     1 RARLSLPRQLYLRQS-ETGAEVGVWTKET-IPVRTCFGPLIGQQShsaevADWTDKAAPHIWKIYHNDVLEFCIITTDEN 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1777535687 312 WANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELG 366
Cdd:cd19189    79 ECNWMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQLG 133
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 237-361 4.25e-18

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: 81.31  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 237 RSALSLPPGLRIGPsgIPQAGLGVWnEASDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYeYVDGKDKSWANWM 316
Cdd:cd19199     2 RARSSLPDNLEIRQ--LEDGSEGVF-ALVPLVKRTQFGPFEAKRVARLDGFAVFPLKVFEKDGSVV-YLDTSNEDDCNWM 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1777535687 317 RYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEY 361
Cdd:cd19199    78 MFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFY 122
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 237-366 1.01e-17

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: 80.09  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 237 RSALSLPPGLRIGPSGIPQagLGVWNEASdLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYE-YVDGKDKSWANW 315
Cdd:cd19194     1 RARASLPLILQIFRFGETL--GGVFAKRR-IPKRTQFGPLEGPLVKKSELKDNKIHPLELEEDDGEDlYFDLSDENKCNW 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1777535687 316 MRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELG 366
Cdd:cd19194    78 MMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 243-360 1.89e-17

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: 79.40  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 243 PPGLRIGPSGIPQAGL--GVWNeASDLPLGLHFGPYEGRITEDEEAANNGyswLITKGRNCYEYVDGKDKSWAN------ 314
Cdd:cd19192     3 HRSLWRGGSKSVLTDIftSVVT-TTDIPAGTIFGPCVLSFTLGYDIADIA---LKTTDKRVVPYIFRVDTGACNgsseps 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1777535687 315 -WMRYVNCARDDEEQNLVAFQY-HRQIFYRTCRVIRPGCELLVWYGDE 360
Cdd:cd19192    79 dWLRLVQPARDRHEQNLEAFRKnEGQVYFRTLRRIRKGEELLVWYSDE 126
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 241-360 2.15e-16

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: 75.92  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 241 SLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGR-----ITEDEEAANNGYSWLITKgRNCYEYVdgkdkswaNW 315
Cdd:cd10520     4 SLPPGLALGPSLAQEERLGVWCVGDALQKGTFLGPLEEEleshdLTEGGSPRQEESGQSGDV-LACEQSS--------KW 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1777535687 316 MRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDE 360
Cdd:cd10520    75 MRFACRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLWPEEN 119
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 221-364 5.77e-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: 70.35  E-value: 5.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 221 PPTFVKDSAVDKGHPNRSALSLPPGLRIGP------SGIPQAGLGVWNEASdLPLGLHFGPYEGRITEDEEAANNGYSWL 294
Cdd:cd19214     3 PATSSEAFTPKEGSPYKAPIYIPDDIPIPSefelreSNIPGTGLGIWTKRK-IEVGEKFGPYVGEQRSNLKDPSYGWEVL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777535687 295 ITKGrNCYEYVDGKDKSWANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWY-GDEYGQE 364
Cdd:cd19214    82 DEFG-NVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMkSEDYSHE 151
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 242-359 6.44e-14

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: 70.29  E-value: 6.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 242 LPPGLRIGPSGIPQAGLGVWNEaSDLPLGLHFGPY---------------EGRITEDEEAANNGYSWLITKGRNCYEY-V 305
Cdd:cd19213    20 IPSDFELRESSIPGAGLGVWAK-RKIEAGERFGPYtgvqrstlkdtnfgwEQILNDVEVSSQEGCITKIVDDLGNEKFcV 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1777535687 306 DGKDKSWANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGD 359
Cdd:cd19213    99 DAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVKD 152
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 240-357 9.19e-14

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: 68.53  E-value: 9.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 240 LSLPPGLR-IGPSGIPQAGLGVWNEAsDLPLGLHFGPYEGRITEDEEaaNNGYSWLIT----KGRNCYEYVDGkDKSwaN 314
Cdd:cd19201     1 LSLPGELElRKPSQDAGRSGGVWAKQ-PLPEGTRFGPYPGKLVKEPL--DPSYEWKVEaqgsKGGEGLLLLTE-DSG--T 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1777535687 315 WMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWY 357
Cdd:cd19201    75 WLKLVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVL 117
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
611-878 5.16e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.42  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 611 RECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRgFSRQSVLLTHQRRHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEK 690
Cdd:COG5048   175 SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 691 PYVCRECGR------GFSWQSVLLTHQRTHTG-EKPYVCRECGRGFSNKSHLLRHQRT--HTGE--KPYVCRE--CGRGF 757
Cdd:COG5048   254 SSSASESPRsslptaSSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 758 RDKSHLLRHQRTHTGEKPYVC--RECGRGFRDKSNLLSHQRTH-----TGEKPYVC--RECGRGFSNKSHLLRHQRTHTG 828
Cdd:COG5048   334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLS 413

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1777535687 829 EKPYVCR--ECGRGFRNKSHLLRHQRTHTGEKPYVCRECGRgFSDRSSLCYH 878
Cdd:COG5048   414 FRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 267-358 9.55e-13

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: 65.23  E-value: 9.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 267 LPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCY-EYVDGKDKSWA-NWMRYVNCARDDEEQNLVAFQYHR--QIFYR 342
Cdd:cd19197     1 IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRgDYLVDESGSPAtEWIGLVRAARNNQEQNLEAIADLPggQIFYR 80

                          90
                  ....*....|....*.
gi 1777535687 343 TCRVIRPGCELLVWYG 358
Cdd:cd19197    81 ALRDIQPGEELTVWYS 96
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 171-201 4.01e-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: 58.16  E-value: 4.01e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1777535687 171 LRKKETERKMYSLRERKGHAYKEVSEPQDDD 201
Cdd:pfam09514   1 LRRKEVEVWMYRLRERKGVVYEEISDPQEDD 31
KRAB smart00349
krueppel associated box;
27-85 1.70e-10

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 57.22  E-value: 1.70e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687   27 AFKDISIYFTKEEWAEMGDWEKTRYRNV-KRNYNALITIGLRATRPAFMCHRRQAIKLQV 85
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVmLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
587-766 4.15e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 587 RGFSWQSVLLTHQRTHTG-EKPYVCRECGRGFSRQSVLLTHQR--RHTGE--KPYVCRE--CGRGFSRQSVLLTHQRRHT 659
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 660 GEKPYVCRECGRGfSWQSVLLT--------HQRTHTGEKPYVC--RECGRGFSWQSVLLTHQRTHTGEKPYVCR--ECGR 727
Cdd:COG5048   348 SISPAKEKLLNSS-SKFSPLLNneppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSK 426

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1777535687 728 GFSNKSHLLRHQRTHTGEKPYVCRECGRgFRDKSHLLRH 766
Cdd:COG5048   427 SFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
592-894 5.98e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 592 QSVLLTHQRTHTGE----KPYVCRECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRG--FSRQSVLLTHQRRHTGEKPYV 665
Cdd:COG5048    14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 666 CRECGR--------------GFSWQSVLLTHQRTHTGEKPYV------------CRECGRGFSWQSVLLTHQRTHtGEKP 719
Cdd:COG5048    94 NSKSLPlsnskasssslsssSSNSNDNNLLSSHSLPPSSRDPqlpdllsisnlrNNPLPGNNSSSVNTPQSNSLH-PPLP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 720 yVCRECGRGFSNKSHLLRHQRTHTGEKPYVCRECGRgFRDKSHLLRHQRTHTGEKPYVCRECGRGFRDKSNLLSHQRTHT 799
Cdd:COG5048   173 -ANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 800 GEKPYVCRECGR------GFSNKSHLLRHQRTHTG-EKPYVCRECGRGFRNKSHLLRHQRT--HTGE--KPYVCRE--CG 866
Cdd:COG5048   251 SDSSSSASESPRsslptaSSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCG 330

                         330       340
                  ....*....|....*....|....*...
gi 1777535687 867 RGFSDRSSLCYHQRTHTGEKPYVCREDE 894
Cdd:COG5048   331 KLFSRNDALKRHILLHTSISPAKEKLLN 358
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 255-359 6.24e-09

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: 54.99  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 255 QAGLGVWNeASDLPLGLHFGPYEG--RITED-EEAANNGYSWLI--TKGRNCYeYVDGKDKSWANWMRYVNCARDDEEQN 329
Cdd:cd19190    17 QDGMGLYT-ARRVKKGEKFGPFAGekRMPNElDESMDPRLMWEVrgSKGEVLY-ILDASNPRHSNWLRFVHEAPSQEQKN 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 1777535687 330 LVAFQYHRQIFYRTCRVIRPGCELLVWYGD 359
Cdd:cd19190    95 LAAIQEGENIFYLAVDDIETDTELLIGYLD 124
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 246-364 2.98e-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: 53.11  E-value: 2.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687  246 LRIGPSgiPQAGLGVWneAS-DLPLGLHFGPYEGRITEDEEAANNG--YSWLITKGRNCYE-----YVDGKDKSwaNWMR 317
Cdd:smart00317   3 LEVFKS--PGKGWGVR--ATeDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFYLFDidsdlCIDARRKG--NLAR 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1777535687  318 YVNCARDDEEQNLVAFQ-YHRQIFYRTCRVIRPGCELLVWYGDEYGQE 364
Cdd:smart00317  77 FINHSCEPNCELLFVEVnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 247-361 4.95e-08

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: 52.34  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 247 RIGPSGIP---QAGLGVWnEASDLPLGLHFGPYEG-RITEDEEAANN----GYSWLITKGRNCYeYVDGKDKswANWMRY 318
Cdd:cd10522     1 KVDISMIPnlsHNGLGLF-AAETIAKGEFVGEYTGeVLDRWEEDRDSvyhyDPLYPFDLNGDIL-VIDAGKK--GNLTRF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1777535687 319 VNCARDDeeqNLVAFQYHRQ----IFYRTCRVIRPGCELLVWYGDEY 361
Cdd:cd10522    77 INHSDQP---NLELIVRTLKgeqhIGFVAIRDIKPGEELFISYGPKY 120
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
559-738 1.40e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 559 RGFSWKSHLLIHQRIHTG-EKPYVCRECGRGFSWQSVLLTHQRT--HTGE--KPYVCRE--CGRGFSRQSVLLTHQRRHT 631
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 632 GEKPYVCRECGRGFSRQSVL-------LTHQRRHTGEKPYVC--RECGRGFSWQSVLLTHQRTHTGEKPYVCR--ECGRG 700
Cdd:COG5048   348 SISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1777535687 701 FSWQSVLLTHQRTHTGEKPYVCRECGRgFSNKSHLLRH 738
Cdd:COG5048   428 FNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 27-62 1.99e-07

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: 47.93  E-value: 1.99e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1777535687  27 AFKDISIYFTKEEWAEMGDWEKTRYRNVKR-NYNALI 62
Cdd:cd07765     2 TFEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
528-671 5.32e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 528 ECGQGFSVKSDVITHQRT--HTGEKL--YVCRE--CGRGFSWKSHLLIHQRIHTGEKPYVCRECGRGfSWQSVLLT---- 597
Cdd:COG5048   294 QCNISFSRSSPLTRHLRSvnHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSS-SKFSPLLNnepp 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 598 ----HQRTHTGEKPYVC--RECGRGFSRQSVLLTHQRRHTGEKPYVCR--ECGRGFSRQSVLLTHQRRHTGEKPYVCREC 669
Cdd:COG5048   373 qslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL 452


                  ..
gi 1777535687 670 GR 671
Cdd:COG5048   453 KS 454
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 28-65 2.71e-06

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: 44.77  E-value: 2.71e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1777535687  28 FKDISIYFTKEEWAEMGDWEKTRYRNV-KRNYNALITIG 65
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQRNLYRDVmLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
811-887 1.53e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 811 RGFSNKSHLL-RHQRTHTGE----KPYVCRECGRGFRNKSHLLRHQRTHTGEKPYVCRECGRG--FSDRSSLCYHQRTHT 883
Cdd:COG5048     8 SSSSNNSVLSsTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHH 87


                  ....
gi 1777535687 884 GEKP 887
Cdd:COG5048    88 NNPS 91
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 298-358 3.07e-05

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: 44.05  E-value: 3.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777535687 298 GRNCYEYVDGKDKSWANWMRYVNcaRDDEEQNLVAFQY---HRQIFYRTCRVIRPGCELLVWYG 358
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFIN--HSCDPNCEVRVVYvngGPRIVIFALRDIKPGEELTIDYG 115
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
727-803 1.23e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 727 RGFSNKSHLL-RHQRTHTGE----KPYVCRECGRGFRDKSHLLRHQRTHTGEKPYVCRECGRG--FRDKSNLLSHQRTHT 799
Cdd:COG5048     8 SSSSNNSVLSsTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHH 87


                  ....
gi 1777535687 800 GEKP 803
Cdd:COG5048    88 NNPS 91
zf-H2C2_2 pfam13465
Zinc-finger double domain;
818-843 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 1777535687 818 HLLRHQRTHTGEKPYVCRECGRGFRN 843
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
846-870 2.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 2.04e-04
                          10        20
                  ....*....|....*....|....*
gi 1777535687 846 HLLRHQRTHTGEKPYVCRECGRGFS 870
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
734-757 2.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.68e-04
                          10        20
                  ....*....|....*....|....
gi 1777535687 734 HLLRHQRTHTGEKPYVCRECGRGF 757
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
762-785 2.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.68e-04
                          10        20
                  ....*....|....*....|....
gi 1777535687 762 HLLRHQRTHTGEKPYVCRECGRGF 785
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
790-815 2.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.90e-04
                          10        20
                  ....*....|....*....|....*.
gi 1777535687 790 NLLSHQRTHTGEKPYVCRECGRGFSN 815
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 720-742 3.48e-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: 3.48e-04
                          10        20
                  ....*....|....*....|...
gi 1777535687 720 YVCRECGRGFSNKSHLLRHQRTH 742
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 804-826 3.48e-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: 3.48e-04
                          10        20
                  ....*....|....*....|...
gi 1777535687 804 YVCRECGRGFSNKSHLLRHQRTH 826
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 832-854 3.65e-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: 3.65e-04
                          10        20
                  ....*....|....*....|...
gi 1777535687 832 YVCRECGRGFRNKSHLLRHQRTH 854
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 748-770 4.23e-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: 4.23e-04
                          10        20
                  ....*....|....*....|...
gi 1777535687 748 YVCRECGRGFRDKSHLLRHQRTH 770
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
595-619 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|....*
gi 1777535687 595 LLTHQRTHTGEKPYVCRECGRGFSR 619
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 776-798 1.31e-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: 36.89  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|...
gi 1777535687 776 YVCRECGRGFRDKSNLLSHQRTH 798
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
623-647 1.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.34e-03
                          10        20
                  ....*....|....*....|....*
gi 1777535687 623 LLTHQRRHTGEKPYVCRECGRGFSR 647
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
707-731 1.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.38e-03
                          10        20
                  ....*....|....*....|....*
gi 1777535687 707 LLTHQRTHTGEKPYVCRECGRGFSN 731
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PR-SET_ZFPM1 cd19215
PR-SET domain found in zinc finger protein ZFPM1 and similar proteins; ZFPM1 (also termed ...
 266-355 1.58e-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: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777535687 266 DLPLGLHFGPYEGRIT----EDEEAANNGYSWLITKGRNCyeyvdgkdkswanWMRYVNCARDDEEQNLVAFQYHRQIFY 341
Cdd:cd19215    23 SLSEGLSWGPYHGSIQssasSPGQAEESPAVTLLLVDEDC-------------WLRRLPLVSTEAEANCTIYRKGDAIWC 89

                          90
                  ....*....|....
gi 1777535687 342 RTCRVIRPGCELLV 355
Cdd:cd19215    90 KTTKPVPEGELLSA 103
zf-H2C2_2 pfam13465
Zinc-finger double domain;
679-702 2.17e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.17e-03
                          10        20
                  ....*....|....*....|....
gi 1777535687 679 LLTHQRTHTGEKPYVCRECGRGFS 702
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
566-590 2.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|....*
gi 1777535687 566 HLLIHQRIHTGEKPYVCRECGRGFS 590
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
651-674 2.72e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.72e-03
                          10        20
                  ....*....|....*....|....
gi 1777535687 651 LLTHQRRHTGEKPYVCRECGRGFS 674
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 860-882 5.93e-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: 34.97  E-value: 5.93e-03
                          10        20
                  ....*....|....*....|...
gi 1777535687 860 YVCRECGRGFSDRSSLCYHQRTH 882
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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