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Conserved domains on  [gi|2129453402|ref|XP_044857580|]
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histone-lysine N-methyltransferase PRDM9-like isoform X3 [Mauremys mutica]

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 ...
 266-394 1.10e-83

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: 262.17  E-value: 1.10e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 266 LTLPPGMRIGLSSIPQAGLGVWNEADtLPIGVHFGPYDGRITEEEEAAHNGYSWLITKGRNWYVYIDGKDETNANWMRYV 345
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEAP-IPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2129453402 346 NCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKELGIK 394
Cdd:cd19193    81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
541-755 6.83e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.65  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 541 YSCGECGQNFHRPShwVRHQQSHTGeKSYPCGECGRRFSHS-----SSLTTHQRIHTGER-----PFQCLECGRRFSQSA 610
Cdd:COG5048   227 LPLTTNSQLSPKSL--LSQSPSSLS-SSDSSSSASESPRSSlptasSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSS 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 611 NLTAHQR--IHTGE--RPFQCLE--CGRRFSQSAKLTTHQRIHTGERPFQCLECGRRFSHSSSLTT-------HQRIHTG 677
Cdd:COG5048   304 PLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKN 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 678 ERPFQCL--ECGRRFSESSSLTRHQRTHTGERP--FQCLECGRRFSHSSSLTAHQRIHTGERPFQClECGRRFSESSHLT 753
Cdd:COG5048   384 DKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLS 462


                  ..
gi 2129453402 754 RH 755
Cdd:COG5048   463 NH 464
KRAB super family cl42959
krueppel associated box;
52-100 1.05e-08

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.21  E-value: 1.05e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2129453402   52 FKELSIYFPKEQWAEMGAWEKTRYRN-MKRNYEFMIELGLPTPKPAFMCR 100
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQKNLYRDvMLENYSNLVSLGFQVPKPDLISQ 52
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
735-787 6.96e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 6.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2129453402 735 RPFQCLECGRRFSESSHLTRHQRTHTGERPFQCSESGRRVRQ--PSNLTGHQRTH 787
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFsrPLELSRHLRTH 86
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 202-227 7.47e-04

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: 37.36  E-value: 7.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 202 TQVNTYSLRKREKKVYVEINEPQDDD 227
Cdd:pfam09514   6 VEVWMYRLRERKGVVYEEISDPQEDD 31
 
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 ...
 266-394 1.10e-83

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: 262.17  E-value: 1.10e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 266 LTLPPGMRIGLSSIPQAGLGVWNEADtLPIGVHFGPYDGRITEEEEAAHNGYSWLITKGRNWYVYIDGKDETNANWMRYV 345
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEAP-IPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2129453402 346 NCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKELGIK 394
Cdd:cd19193    81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
541-755 6.83e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.65  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 541 YSCGECGQNFHRPShwVRHQQSHTGeKSYPCGECGRRFSHS-----SSLTTHQRIHTGER-----PFQCLECGRRFSQSA 610
Cdd:COG5048   227 LPLTTNSQLSPKSL--LSQSPSSLS-SSDSSSSASESPRSSlptasSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSS 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 611 NLTAHQR--IHTGE--RPFQCLE--CGRRFSQSAKLTTHQRIHTGERPFQCLECGRRFSHSSSLTT-------HQRIHTG 677
Cdd:COG5048   304 PLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKN 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 678 ERPFQCL--ECGRRFSESSSLTRHQRTHTGERP--FQCLECGRRFSHSSSLTAHQRIHTGERPFQClECGRRFSESSHLT 753
Cdd:COG5048   384 DKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLS 462


                  ..
gi 2129453402 754 RH 755
Cdd:COG5048   463 NH 464
KRAB smart00349
krueppel associated box;
52-100 1.05e-08

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.21  E-value: 1.05e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2129453402   52 FKELSIYFPKEQWAEMGAWEKTRYRN-MKRNYEFMIELGLPTPKPAFMCR 100
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQKNLYRDvMLENYSNLVSLGFQVPKPDLISQ 52
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 273-390 3.06e-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: 52.72  E-value: 3.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402  273 RIGLSSIPQAGLGVWNeADTLPIGVHFGPYDGRITEEEEAAHNG--YSWLITKGR-----NWYVYIDGKDEtnANWMRYV 345
Cdd:smart00317   2 KLEVFKSPGKGWGVRA-TEDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFylfdiDSDLCIDARRK--GNLARFI 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2129453402  346 NCARDEEEQNLVAFQ-YHGKIYYRVCRAILPHCELLVWYGDEYGKE 390
Cdd:smart00317  79 NHSCEPNCELLFVEVnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
735-787 6.96e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 6.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2129453402 735 RPFQCLECGRRFSESSHLTRHQRTHTGERPFQCSESGRRVRQ--PSNLTGHQRTH 787
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFsrPLELSRHLRTH 86
zf-H2C2_2 pfam13465
Zinc-finger double domain;
695-720 2.87e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.87e-05
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 695 SLTRHQRTHTGERPFQCLECGRRFSH 720
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 679-731 6.20e-05

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: 42.16  E-value: 6.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 679 RPFqCLECGRRFSESSSLTRHQRTHTgerpFQCLECGRRFSHSSSLTAH-QRIH 731
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 52-88 6.92e-05

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: 40.61  E-value: 6.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2129453402  52 FKELSIYFPKEQWAEMGAWEKTRYRNMKR-NYEFMIEL 88
Cdd:cd07765     3 FEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 52-89 3.18e-04

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: 38.61  E-value: 3.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2129453402  52 FKELSIYFPKEQWAEMGAWEKTRYRN-MKRNYEFMIELG 89
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQRNLYRDvMLENYRNLVSLG 42
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 324-384 6.87e-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: 40.20  E-value: 6.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129453402 324 GRNWYVYIDGKDETNANWMRYVN--CardeeEQNLVAF----QYHGKIYYRVCRAILPHCELLVWYG 384
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFINhsC-----DPNCEVRvvyvNGGPRIVIFALRDIKPGEELTIDYG 115
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 202-227 7.47e-04

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: 37.36  E-value: 7.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 202 TQVNTYSLRKREKKVYVEINEPQDDD 227
Cdd:pfam09514   6 VEVWMYRLRERKGVVYEEISDPQEDD 31
 
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 ...
 266-394 1.10e-83

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: 262.17  E-value: 1.10e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 266 LTLPPGMRIGLSSIPQAGLGVWNEADtLPIGVHFGPYDGRITEEEEAAHNGYSWLITKGRNWYVYIDGKDETNANWMRYV 345
Cdd:cd19193     2 LTLPPGLSIKRSSIPGAGLGVWAEAP-IPKGMVFGPYEGEIVEDEEAADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2129453402 346 NCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKELGIK 394
Cdd:cd19193    81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKELGIK 129
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 268-393 5.00e-34

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: 126.70  E-value: 5.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 268 LPPGMRIGLSSIPQAGLGVWNeADTLPIGVHFGPYDGRI---TEEEEAAHNGYSW--LITKGRNWYvYIDGKDETNANWM 342
Cdd:cd19196     1 LPSQVIIAQSSIPGAGLGVFS-KTWIKEGTEMGPYTGRIvspEDVDPCKNNNLMWevFNEDGTVSH-FIDASQENHRSWM 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2129453402 343 RYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKELGI 393
Cdd:cd19196    79 TFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTFLGI 129
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 264-391 1.93e-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: 124.97  E-value: 1.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 264 AALTLPPGMRIGLSSIPQAGLGVWNEAdtLPIGVHFGPYDGRITEEEEAAhNGYSWLITKGRNWYVYIDGKDETNANWMR 343
Cdd:cd19195     1 AALTAPQGIEVVKDTSGESDVRCVDEV--IPKGHIFGPYEGQICTQDKSS-GFFSWLIVDKNNRYKSIDGSDETKANWMR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2129453402 344 YVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKEL 391
Cdd:cd19195    78 YVVISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRL 125
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 266-393 3.09e-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: 121.74  E-value: 3.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 266 LTLPPGMRI---GLSSIPQAGLGVwneADTLPIGVHFGPYDGRI---TEEEEAAHNGYSWLITKGRNWYVYIDGKDETnA 339
Cdd:cd19198     1 LDLPEGLRVlqtSFGGTPHYGVFC---KKTIPKGTRFGPFRGRVvntSEIKTYDDNSFMWEIFEDGKLSHFIDGRGST-G 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 340 NWMRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKELGI 393
Cdd:cd19198    77 NWMSYVNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVWYGDCYLQFMGI 130
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 268-384 2.21e-31

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: 117.30  E-value: 2.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 268 LPPGMRIGLSSIPQAGLGVWNeADTLPIGVHFGPYDGRIteeeeaahngyswlitkgrnwyvyidgkdetnaNWMRYVNC 347
Cdd:cd10534     1 LPAGLELVLSSIPEGGLGVFA-RRTIPAGTRFGPLEGVV---------------------------------NWMRFVRP 46

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2129453402 348 ARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYG 384
Cdd:cd10534    47 ARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWYS 83
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 267-391 1.09e-28

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: 111.26  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 267 TLPPGMRIGLSSIPQAGLGVWNEaDTLPIGVHFGPYDGRITEEEEAAHNG---YSWLITKGRNWYVYIDGKDETNANWMR 343
Cdd:cd19187     2 SLPRNLTLKYSSVGREVLGVWSS-DYIPRGTRFGPLVGEIYTNDPVPKGAnrkYFWRIYSNGEFYHYIDGFDPSKSNWMR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2129453402 344 YVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKEL 391
Cdd:cd19187    81 YVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 268-387 4.21e-27

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: 106.79  E-value: 4.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 268 LPPGMRIGLSSIPQAGLGVWnEADTLPIGVHFGPYDG-RITEEEEAA---HNGYSWLI--TKGRNWYvYIDGKDETNANW 341
Cdd:cd19191     1 LPDEVCLCTSSIPGLGYGIC-AAQRIPQGTWIGPFEGvLVSPEKQIGavrNTQHLWEIydQEGTLQH-FIDGGDPSKSSW 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2129453402 342 MRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEY 387
Cdd:cd19191    79 MRYIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLVWYDDSY 124
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 268-386 6.58e-26

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: 103.29  E-value: 6.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 268 LPPGMRIGLSSIPQAGLGVWNeADTLPIGVHFGPYDGRITEEEEAAHNGYSW-LITKGRNWYVyIDGKDETNANWMRYVN 346
Cdd:cd19188     4 LPEELELKPSAVDKTRIGVWA-KKSIPKGRKFGPFVGEKKKRSQVKNNVYMWeIYGPKRGWMC-VDASDPTKGNWLRYVN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2129453402 347 CARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDE 386
Cdd:cd19188    82 WARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWYNGE 121
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 263-392 5.71e-24

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: 97.92  E-value: 5.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 263 RAALTLPPGMRIGlSSIPQAGLGVWNEaDTLPIGVHFGPYDGRITEEEEAAhngySWLiTKGRN--WYVY--------ID 332
Cdd:cd19189     1 RARLSLPRQLYLR-QSETGAEVGVWTK-ETIPVRTCFGPLIGQQSHSAEVA----DWT-DKAAPhiWKIYhndvlefcII 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 333 GKDETNANWMRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKELG 392
Cdd:cd19189    74 TTDENECNWMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQLG 133
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 263-392 6.08e-20

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


Pssm-ID: 380971  Cd Length: 128  Bit Score: 86.25  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 263 RAALTLPPGM---RIGLSSipqagLGVWNEAdTLPIGVHFGPYDGRITEEEEAAHNGYSWLITKGRNWY-VYIDGKDETN 338
Cdd:cd19194     1 RARASLPLILqifRFGETL-----GGVFAKR-RIPKRTQFGPLEGPLVKKSELKDNKIHPLELEEDDGEdLYFDLSDENK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 339 ANWMRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKELG 392
Cdd:cd19194    75 CNWMMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFLG 128
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 268-386 7.89e-20

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: 86.27  E-value: 7.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 268 LPPGMRIGLSSIPQAGLGVWNEADtLPIGVHFGPYDGriTEEEEAAHNGYSW-LITKGRNWYVYIDGKDETNANWMRYVN 346
Cdd:cd19200    10 IPPDFELRESAAVGAGLGVWTKVR-IEVGEKFGPFVG--VQRSSVKDPTYAWeIVDEFGKVKFWIDASEPGTGNWMKYIR 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2129453402 347 CARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDE 386
Cdd:cd19200    87 SAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAA 126
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 267-386 3.38e-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: 80.93  E-value: 3.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 267 TLPPGMRIGLSSIPQAGLGVWNEADTLPIGVHFGPYdgritEEEEAAHngyswLITKGRNWYVYIDGKD------ETNAN 340
Cdd:cd10520     4 SLPPGLALGPSLAQEERLGVWCVGDALQKGTFLGPL-----EEELESH-----DLTEGGSPRQEESGQSgdvlacEQSSK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2129453402 341 WMRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDE 386
Cdd:cd10520    74 WMRFACRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLWPEEN 119
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 263-391 3.44e-16

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: 75.53  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 263 RAALTLPPGMRIglSSIPQAGLGVWneADT-LPIGVHFGPYDGRITEEEEAAHNGYSWLITKGRNwYVYIDGKDETNANW 341
Cdd:cd19199     2 RARSSLPDNLEI--RQLEDGSEGVF--ALVpLVKRTQFGPFEAKRVARLDGFAVFPLKVFEKDGS-VVYLDTSNEDDCNW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2129453402 342 MRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDEYGKEL 391
Cdd:cd19199    77 MMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 241-385 8.06e-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: 72.60  E-value: 8.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 241 ECSVHGPPAFIKDPIvetgqerraalTLPPGMRIGLSSIPQAGLGVWNEAdTLPIGVHFGPYDG---------------R 305
Cdd:cd19213     4 EGSPYEAPVYIPDDI-----------PIPSDFELRESSIPGAGLGVWAKR-KIEAGERFGPYTGvqrstlkdtnfgweqI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 306 ITEEEEAAHNGYSWLITKGR-NWYVYIDGKDETNANWMRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYG 384
Cdd:cd19213    72 LNDVEVSSQEGCITKIVDDLgNEKFCVDAGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVK 151


                  .
gi 2129453402 385 D 385
Cdd:cd19213   152 D 152
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 285-383 2.59e-13

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: 66.98  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 285 GVWNEADtLPIGVHFGPYDGRITEEEEAAHngYSWLITK-GRNWYVYIDGKDETNANWMRYVNCARDEEEQNLVAFQYHG 363
Cdd:cd19201    21 GVWAKQP-LPEGTRFGPYPGKLVKEPLDPS--YEWKVEAqGSKGGEGLLLLTEDSGTWLKLVRSADDEDEANLILYFKGG 97

                          90       100
                  ....*....|....*....|
gi 2129453402 364 KIYYRVCRAILPHCELLVWY 383
Cdd:cd19201    98 QIWCEVTKDIPPGEELILVL 117
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
541-755 6.83e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.65  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 541 YSCGECGQNFHRPShwVRHQQSHTGeKSYPCGECGRRFSHS-----SSLTTHQRIHTGER-----PFQCLECGRRFSQSA 610
Cdd:COG5048   227 LPLTTNSQLSPKSL--LSQSPSSLS-SSDSSSSASESPRSSlptasSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSS 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 611 NLTAHQR--IHTGE--RPFQCLE--CGRRFSQSAKLTTHQRIHTGERPFQCLECGRRFSHSSSLTT-------HQRIHTG 677
Cdd:COG5048   304 PLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKN 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 678 ERPFQCL--ECGRRFSESSSLTRHQRTHTGERP--FQCLECGRRFSHSSSLTAHQRIHTGERPFQClECGRRFSESSHLT 753
Cdd:COG5048   384 DKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLS 462


                  ..
gi 2129453402 754 RH 755
Cdd:COG5048   463 NH 464
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 285-386 1.76e-12

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: 65.14  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 285 GVWNEADtLPIGVHFGPYDGRITEEEEAAHNGyswLITKGRNWYVYIDGKDETNAN-------WMRYVNCARDEEEQNLV 357
Cdd:cd19192    21 SVVTTTD-IPAGTIFGPCVLSFTLGYDIADIA---LKTTDKRVVPYIFRVDTGACNgssepsdWLRLVQPARDRHEQNLE 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 2129453402 358 AFQY-HGKIYYRVCRAILPHCELLVWYGDE 386
Cdd:cd19192    97 AFRKnEGQVYFRTLRRIRKGEELLVWYSDE 126
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 237-386 4.71e-12

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: 64.57  E-value: 4.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 237 FFIDECSVHGPPAFIKDPIvetgqerraalTLPPGMRIGLSSIPQAGLGVWNEADtLPIGVHFGPYDGRitEEEEAAHNG 316
Cdd:cd19214    10 FTPKEGSPYKAPIYIPDDI-----------PIPSEFELRESNIPGTGLGIWTKRK-IEVGEKFGPYVGE--QRSNLKDPS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129453402 317 YSW-LITKGRNWYVYIDGKDETNANWMRYVNCARDEEEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGDE 386
Cdd:cd19214    76 YGWeVLDEFGNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMKSE 146
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
463-787 3.63e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 3.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 463 LSFPGDPPSQQLPPDPSSLHKGTWGKKPHLQGQREGVGGREAFGLLSNLPPQQWRdTTGEPHAQSETGEAGGGGRRQKYS 542
Cdd:COG5048   123 LSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLS-KDPSSNLSLLISSNVSTSIPSSSE 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 543 CGECGQNFHRPSHwVRHQQSHTGEKSYPCGECGRRFSHSSSLTTHQRIHTGERPFQCLECGRRFSQSANLTAHQRIHTGE 622
Cdd:COG5048   202 NSPLSSSYSIPSS-SSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDS 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 623 rpfqclecgrrfsqsaklTTHQRIHTgerPFQCLECGRRFSHSSSLTTHQR--IHTGE--RPFQCLE--CGRRFSESSSL 696
Cdd:COG5048   281 ------------------SSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDAL 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 697 TRHQRTHTGERPFQCLECGRRFSHSSSLTA-------HQRIHTGERPFQCL--ECGRRFSESSHLTRHQRTHTGERPFQC 767
Cdd:COG5048   340 KRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC 419

                         330       340
                  ....*....|....*....|..
gi 2129453402 768 SESGR--RVRQPSNLTGHQRTH 787
Cdd:COG5048   420 KNPPCskSFNRHYNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
541-787 1.76e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.95  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 541 YSCGECGQNFHRPSHWVRHQQSHTGEKSYPCGECGR--RFSHSSSLTTHQRIHTGERPF--------------------- 597
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHNNPSDlnskslplsnskasssslsss 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 598 ---------------------------------------QCLECGRRFSQSANL-------------------TAHQRIH 619
Cdd:COG5048   114 ssnsndnnllsshslppssrdpqlpdllsisnlrnnplpGNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVS 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 620 TGERPFQCLECGRRFSQSAKLTTHQRIHTGERPFQCLECGRRFSHSSSLTTHQRIHTGERPFQCLECGRRF--SESSSLT 697
Cdd:COG5048   194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSlpTASSQSS 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 698 RHQRTHTGER-----PFQCLECGRRFSHSSSLTAHQR--IHTGE--RPFQCLE--CGRRFSESSHLTRHQRTHTGERPFQ 766
Cdd:COG5048   274 SPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                         330       340
                  ....*....|....*....|...
gi 2129453402 767 CSESGRRVRQPSNLTG--HQRTH 787
Cdd:COG5048   354 EKLLNSSSKFSPLLNNepPQSLQ 376
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 331-384 2.93e-10

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: 57.91  E-value: 2.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2129453402 331 IDGKDETNANWMRYVNCARDEEEQNLVAFQ--YHGKIYYRVCRAILPHCELLVWYG 384
Cdd:cd19197    41 VDESGSPATEWIGLVRAARNNQEQNLEAIAdlPGGQIFYRALRDIQPGEELTVWYS 96
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
536-699 5.57e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 536 GRRQKYSCGECGQNFHRPSHWVRHQQS--HTGEKSYPCGE----CGRRFSHSSSLTTHQRIHTGERPFQCLECGRRFSQS 609
Cdd:COG5048   285 GFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGESLKPFSCpyslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFS 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 610 ANLTA-------HQRIHTGERPFQCL--ECGRRFSQSAKLTTHQRIHTGERP--FQCLECGRRFSHSSSLTTHQRIHTGE 678
Cdd:COG5048   365 PLLNNeppqslqQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNH 444

                         170       180
                  ....*....|....*....|.
gi 2129453402 679 RPFQClECGRRFSESSSLTRH 699
Cdd:COG5048   445 APLLC-SILKSFRRDLDLSNH 464
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 277-385 1.16e-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: 56.92  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 277 SSIPQAGLGVWNeADTLPIGVHFGPYDG--RITEE-EEAAHNGYSWLI--TKGRNWYVyIDGKDETNANWMRYVNCARDE 351
Cdd:cd19190    13 SSKVQDGMGLYT-ARRVKKGEKFGPFAGekRMPNElDESMDPRLMWEVrgSKGEVLYI-LDASNPRHSNWLRFVHEAPSQ 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129453402 352 EEQNLVAFQYHGKIYYRVCRAILPHCELLVWYGD 385
Cdd:cd19190    91 EQKNLAAIQEGENIFYLAVDDIETDTELLIGYLD 124
KRAB smart00349
krueppel associated box;
52-100 1.05e-08

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.21  E-value: 1.05e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2129453402   52 FKELSIYFPKEQWAEMGAWEKTRYRN-MKRNYEFMIELGLPTPKPAFMCR 100
Cdd:smart00349   3 FEDVAVYFTQEEWEQLDPAQKNLYRDvMLENYSNLVSLGFQVPKPDLISQ 52
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 273-390 3.06e-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: 52.72  E-value: 3.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402  273 RIGLSSIPQAGLGVWNeADTLPIGVHFGPYDGRITEEEEAAHNG--YSWLITKGR-----NWYVYIDGKDEtnANWMRYV 345
Cdd:smart00317   2 KLEVFKSPGKGWGVRA-TEDIPKGEFIGEYVGEIITSEEAEERPkaYDTDGAKAFylfdiDSDLCIDARRK--GNLARFI 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2129453402  346 NCARDEEEQNLVAFQ-YHGKIYYRVCRAILPHCELLVWYGDEYGKE 390
Cdd:smart00317  79 NHSCEPNCELLFVEVnGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 273-387 5.00e-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: 51.96  E-value: 5.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 273 RIGLSSIP---QAGLGVWnEADTLPIGVHFGPYDGRIT--EEEEAA---HNGYSWLITKGRNwYVYIDGKDEtnANWMRY 344
Cdd:cd10522     1 KVDISMIPnlsHNGLGLF-AAETIAKGEFVGEYTGEVLdrWEEDRDsvyHYDPLYPFDLNGD-ILVIDAGKK--GNLTRF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2129453402 345 VNCARD---EEEQNLVAFQYHgkIYYRVCRAILPHCELLVWYGDEY 387
Cdd:cd10522    77 INHSDQpnlELIVRTLKGEQH--IGFVAIRDIKPGEELFISYGPKY 120
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
635-704 1.19e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 1.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129453402 635 SQSAKLTTHQRIHTGE----RPFQCLECGRRFSHSSSLTTHQRIHTGERPFQCLECGR--RFSESSSLTRHQRTHT 704
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHH 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
693-768 4.29e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129453402 693 SSSLTRHQRTHTGE----RPFQCLECGRRFSHSSSLTAHQRIHTGERPFQCLECGR--RFSESSHLTRHQRTHTGERPFQ 766
Cdd:COG5048    14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHNNPSDL 93


                  ..
gi 2129453402 767 CS 768
Cdd:COG5048    94 NS 95
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
607-676 4.44e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 4.44e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129453402 607 SQSANLTAHQRIHTGE----RPFQCLECGRRFSQSAKLTTHQRIHTGERPFQCLECGR--RFSHSSSLTTHQRIHT 676
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHH 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
665-732 5.65e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 5.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 665 SSSLTTHQRIHTGE----RPFQCLECGRRFSESSSLTRHQRTHTGERPFQCLECGR--RFSHSSSLTAHQRIHT 732
Cdd:COG5048    14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHH 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
735-787 6.96e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 6.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2129453402 735 RPFQCLECGRRFSESSHLTRHQRTHTGERPFQCSESGRRVRQ--PSNLTGHQRTH 787
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFsrPLELSRHLRTH 86
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
581-648 1.27e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 1.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 581 SSSLTTHQRIHTGE----RPFQCLECGRRFSQSANLTAHQRIHTGERPFQCLECGR--RFSQSAKLTTHQRIHT 648
Cdd:COG5048    14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
695-720 2.87e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.87e-05
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 695 SLTRHQRTHTGERPFQCLECGRRFSH 720
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 679-731 6.20e-05

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: 42.16  E-value: 6.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 679 RPFqCLECGRRFSESSSLTRHQRTHTgerpFQCLECGRRFSHSSSLTAH-QRIH 731
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 52-88 6.92e-05

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: 40.61  E-value: 6.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2129453402  52 FKELSIYFPKEQWAEMGAWEKTRYRNMKR-NYEFMIEL 88
Cdd:cd07765     3 FEDVAVYFSQEEWELLDPAQRDLYRDVMLeNYENLVSL 40
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 737-759 1.35e-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: 39.59  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|...
gi 2129453402 737 FQCLECGRRFSESSHLTRHQRTH 759
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
611-636 1.51e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.51e-04
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 611 NLTAHQRIHTGERPFQCLECGRRFSQ 636
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
583-608 1.66e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.66e-04
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 583 SLTTHQRIHTGERPFQCLECGRRFSQ 608
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
640-664 2.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.25e-04
                          10        20
                  ....*....|....*....|....*
gi 2129453402 640 LTTHQRIHTGERPFQCLECGRRFSH 664
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 709-731 2.53e-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: 38.82  E-value: 2.53e-04
                          10        20
                  ....*....|....*....|...
gi 2129453402 709 FQCLECGRRFSHSSSLTAHQRIH 731
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 623-675 2.80e-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: 40.23  E-value: 2.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 623 RPFqCLECGRRFSQSAKLTTHQRIHTgerpFQCLECGRRFSHSSSLTTH-QRIH 675
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 681-703 3.10e-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: 3.10e-04
                          10        20
                  ....*....|....*....|...
gi 2129453402 681 FQCLECGRRFSESSSLTRHQRTH 703
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 52-89 3.18e-04

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: 38.61  E-value: 3.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2129453402  52 FKELSIYFPKEQWAEMGAWEKTRYRN-MKRNYEFMIELG 89
Cdd:pfam01352   4 FEDVAVDFTQEEWALLDPAQRNLYRDvMLENYRNLVSLG 42
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 653-675 3.23e-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: 38.44  E-value: 3.23e-04
                          10        20
                  ....*....|....*....|...
gi 2129453402 653 FQCLECGRRFSHSSSLTTHQRIH 675
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 597-619 3.63e-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: 3.63e-04
                          10        20
                  ....*....|....*....|...
gi 2129453402 597 FQCLECGRRFSQSANLTAHQRIH 619
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 707-755 3.68e-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: 39.85  E-value: 3.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2129453402 707 RPFqCLECGRRFSHSSSLTAHQRIHTgerpFQCLECGRRFSESSHLTRH 755
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
667-691 3.72e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.72e-04
                          10        20
                  ....*....|....*....|....*
gi 2129453402 667 SLTTHQRIHTGERPFQCLECGRRFS 691
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 569-591 4.42e-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: 4.42e-04
                          10        20
                  ....*....|....*....|...
gi 2129453402 569 YPCGECGRRFSHSSSLTTHQRIH 591
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 324-384 6.87e-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: 40.20  E-value: 6.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129453402 324 GRNWYVYIDGKDETNANWMRYVN--CardeeEQNLVAF----QYHGKIYYRVCRAILPHCELLVWYG 384
Cdd:pfam00856  54 DEDSEYCIDARALYYGNWARFINhsC-----DPNCEVRvvyvNGGPRIVIFALRDIKPGEELTIDYG 115
SSXRD pfam09514
SSXRD motif; SSX1 can repress transcription, and this has been attributed to a putative ...
 202-227 7.47e-04

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: 37.36  E-value: 7.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 202 TQVNTYSLRKREKKVYVEINEPQDDD 227
Cdd:pfam09514   6 VEVWMYRLRERKGVVYEEISDPQEDD 31
zf-H2C2_2 pfam13465
Zinc-finger double domain;
723-747 8.31e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 8.31e-04
                          10        20
                  ....*....|....*....|....*
gi 2129453402 723 SLTAHQRIHTGERPFQCLECGRRFS 747
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 625-647 1.74e-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: 1.74e-03
                          10        20
                  ....*....|....*....|...
gi 2129453402 625 FQCLECGRRFSQSAKLTTHQRIH 647
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-580 2.52e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.52e-03
                          10        20
                  ....*....|....*....|....*.
gi 2129453402 555 HWVRHQQSHTGEKSYPCGECGRRFSH 580
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 574-619 2.94e-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: 37.15  E-value: 2.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2129453402 574 CGRRFSHSSSLTTHQRIHTgerpFQCLECGRRFSQSANLTAH-QRIH 619
Cdd:cd20908     7 CDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 595-647 3.37e-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: 37.15  E-value: 3.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129453402 595 RPFqCLECGRRFSQSANLTAHQRIHTgerpFQCLECGRRFSQSAKLTTH-QRIH 647
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
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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