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Conserved domains on  [gi|568964813|ref|XP_006512567|]
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PR domain zinc finger protein 1 isoform X6 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1-50 2.12e-33

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


The actual alignment was detected with superfamily member cd19187:

Pssm-ID: 394802  Cd Length: 128  Bit Score: 124.36  E-value: 2.12e-33
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19187   79 MRYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-483 9.97e-06

Zinc-finger double domain;


:

Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 42.34  E-value: 9.97e-06
                          10        20
                  ....*....|....*....|....*.
gi 568964813  458 HLQKHYLVHTGEKPHECQVCHKRFSS 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
486-511 1.61e-05

Zinc-finger double domain;


:

Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 41.96  E-value: 1.61e-05
                          10        20
                  ....*....|....*....|....*.
gi 568964813  486 NLKTHLRLHSGEKPYQCKVCPAKFTQ 511
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-455 7.29e-05

Zinc-finger double domain;


:

Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 40.03  E-value: 7.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 568964813  430 NLKVHLRVHSGERPFKCQTCNKGFTQ 455
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
514-539 1.37e-04

Zinc-finger double domain;


:

Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 39.26  E-value: 1.37e-04
                          10        20
                  ....*....|....*....|....*.
gi 568964813  514 HLKLHKRLHTRERPHKCAQCHKSYIH 539
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
247-529 1.56e-04

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 247 SYNAHYPKFLLPPYGISSNGLSTMNNINGINNFSLFPRLYPVYSNLLSGSSLPHPMLN-----PASLPSSLPTDGARRLL 321
Cdd:COG5048   99 PLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSssvntPQSNSLHPPLPANSLSK 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 322 PPEHPKEVLIPAPHSAFSLTGAAASMKDESSPPSGSptagtaatSEHVVQPKATSSVMAAPSTDGAMNLIKNKRNMTGYK 401
Cdd:COG5048  179 DPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSS--------SSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 402 TLPYPlkkqNGKIKYECNVCAKTFGQLSNLKVHLRVHSGER-PFKCQTCNKGFTQLAHLQKHY--LVHTGE--KPHEC-- 474
Cdd:COG5048  251 SDSSS----SASESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpy 326
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568964813 475 QVCHKRFSSTSNLKTHLRLHSGEKPYQCK--VCPAKFTQFVHLKLHKRLHTRERPHK 529
Cdd:COG5048  327 SLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLKN 383
 
Name Accession Description Interval E-value
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
1-50 2.12e-33

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


Pssm-ID: 380964  Cd Length: 128  Bit Score: 124.36  E-value: 2.12e-33
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19187   79 MRYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1-48 5.29e-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: 51.57  E-value: 5.29e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568964813     1 MRYVNPAHSAREQNLAACQNGMN-IYFYTIKPIPANQELLVWYCRDFAE 48
Cdd:smart00317  75 ARFINHSCEPNCELLFVEVNGDDrIVIFALRDIKPGEELTIDYGSDYAN 123
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-483 9.97e-06

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 42.34  E-value: 9.97e-06
                          10        20
                  ....*....|....*....|....*.
gi 568964813  458 HLQKHYLVHTGEKPHECQVCHKRFSS 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
486-511 1.61e-05

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 41.96  E-value: 1.61e-05
                          10        20
                  ....*....|....*....|....*.
gi 568964813  486 NLKTHLRLHSGEKPYQCKVCPAKFTQ 511
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-455 7.29e-05

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 40.03  E-value: 7.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 568964813  430 NLKVHLRVHSGERPFKCQTCNKGFTQ 455
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
514-539 1.37e-04

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 39.26  E-value: 1.37e-04
                          10        20
                  ....*....|....*....|....*.
gi 568964813  514 HLKLHKRLHTRERPHKCAQCHKSYIH 539
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1-42 1.52e-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: 425911  Cd Length: 117  Bit Score: 41.74  E-value: 1.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568964813    1 MRYVNpaHSaREQNLAA----CQNGMNIYFYTIKPIPANQELLVWY 42
Cdd:pfam00856  74 ARFIN--HS-CDPNCEVrvvvVNGGPRIVIFALRDIKPGEELTIDY 116
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
247-529 1.56e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 247 SYNAHYPKFLLPPYGISSNGLSTMNNINGINNFSLFPRLYPVYSNLLSGSSLPHPMLN-----PASLPSSLPTDGARRLL 321
Cdd:COG5048   99 PLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSssvntPQSNSLHPPLPANSLSK 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 322 PPEHPKEVLIPAPHSAFSLTGAAASMKDESSPPSGSptagtaatSEHVVQPKATSSVMAAPSTDGAMNLIKNKRNMTGYK 401
Cdd:COG5048  179 DPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSS--------SSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 402 TLPYPlkkqNGKIKYECNVCAKTFGQLSNLKVHLRVHSGER-PFKCQTCNKGFTQLAHLQKHY--LVHTGE--KPHEC-- 474
Cdd:COG5048  251 SDSSS----SASESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpy 326
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568964813 475 QVCHKRFSSTSNLKTHLRLHSGEKPYQCK--VCPAKFTQFVHLKLHKRLHTRERPHK 529
Cdd:COG5048  327 SLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLKN 383
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
416-438 1.12e-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: 1.12e-03
                          10        20
                  ....*....|....*....|...
gi 568964813  416 YECNVCAKTFGQLSNLKVHLRVH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
442-494 4.34e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.38  E-value: 4.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568964813 442 RPFkCQTCNKGFTQLAHLQ-----KHYlvhtgekphECQVCHKRFSSTSNLKTH-LRLH 494
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIqhqkaKHF---------KCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
1-50 2.12e-33

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


Pssm-ID: 380964  Cd Length: 128  Bit Score: 124.36  E-value: 2.12e-33
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19187   79 MRYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARRL 128
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
1-42 5.78e-17

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: 76.08  E-value: 5.78e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWY 42
Cdd:cd10534   41 MRFVRPARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWY 82
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
1-50 3.57e-15

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  Cd Length: 129  Bit Score: 72.27  E-value: 3.57e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19193   77 MRYVNCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAKEL 126
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
1-50 4.19e-14

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: 69.30  E-value: 4.19e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19194   78 MMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFL 127
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
1-53 2.52e-12

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  Cd Length: 130  Bit Score: 64.30  E-value: 2.52e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYP 53
Cdd:cd19196   78 MTFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTFLGIP 130
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
1-50 6.62e-12

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: 63.25  E-value: 6.62e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19189   83 MMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQL 132
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
1-42 2.42e-10

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: 58.61  E-value: 2.42e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWY 42
Cdd:cd19188   77 LRYVNWARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWY 118
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
1-42 3.10e-10

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: 58.56  E-value: 3.10e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWY 42
Cdd:cd19198   79 MSYVNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVWY 120
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
1-50 7.05e-10

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: 57.04  E-value: 7.05e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19199   77 MMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
1-50 1.27e-08

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: 53.59  E-value: 1.27e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568964813   1 MRYVNPAHSAREQNLAA-CQNGMNIYFYTIKPIPANQELLVWYCRDFAERL 50
Cdd:cd19192   81 LRLVQPARDRHEQNLEAfRKNEGQVYFRTLRRIRKGEELLVWYSDELAELL 131
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1-48 5.29e-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: 51.57  E-value: 5.29e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568964813     1 MRYVNPAHSAREQNLAACQNGMN-IYFYTIKPIPANQELLVWYCRDFAE 48
Cdd:smart00317  75 ARFINHSCEPNCELLFVEVNGDDrIVIFALRDIKPGEELTIDYGSDYAN 123
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
1-51 6.58e-08

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: 51.78  E-value: 6.58e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLH 51
Cdd:cd19195   76 MRYVVISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRLH 126
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
1-42 9.42e-07

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: 48.24  E-value: 9.42e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWY 42
Cdd:cd19191   79 MRYIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLVWY 120
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
1-41 1.88e-06

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: 48.33  E-value: 1.88e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVW 41
Cdd:cd19213  109 LKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVY 149
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
1-46 2.79e-06

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: 46.95  E-value: 2.79e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDF 46
Cdd:cd19201   76 LKLVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLREPL 121
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-483 9.97e-06

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 42.34  E-value: 9.97e-06
                          10        20
                  ....*....|....*....|....*.
gi 568964813  458 HLQKHYLVHTGEKPHECQVCHKRFSS 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
486-511 1.61e-05

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 41.96  E-value: 1.61e-05
                          10        20
                  ....*....|....*....|....*.
gi 568964813  486 NLKTHLRLHSGEKPYQCKVCPAKFTQ 511
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
1-42 3.71e-05

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: 42.88  E-value: 3.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568964813   1 MRYVNPAHSAREQNLAACQN--GMNIYFYTIKPIPANQELLVWY 42
Cdd:cd19197   52 IGLVRAARNNQEQNLEAIADlpGGQIFYRALRDIQPGEELTVWY 95
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
1-40 4.72e-05

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: 43.51  E-value: 4.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLV 40
Cdd:cd19200   82 MKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLL 121
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-455 7.29e-05

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 40.03  E-value: 7.29e-05
                          10        20
                  ....*....|....*....|....*.
gi 568964813  430 NLKVHLRVHSGERPFKCQTCNKGFTQ 455
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
514-539 1.37e-04

Zinc-finger double domain;


Pssm-ID: 433230 [Multi-domain]  Cd Length: 26  Bit Score: 39.26  E-value: 1.37e-04
                          10        20
                  ....*....|....*....|....*.
gi 568964813  514 HLKLHKRLHTRERPHKCAQCHKSYIH 539
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1-42 1.52e-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: 425911  Cd Length: 117  Bit Score: 41.74  E-value: 1.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568964813    1 MRYVNpaHSaREQNLAA----CQNGMNIYFYTIKPIPANQELLVWY 42
Cdd:pfam00856  74 ARFIN--HS-CDPNCEVrvvvVNGGPRIVIFALRDIKPGEELTIDY 116
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
247-529 1.56e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 247 SYNAHYPKFLLPPYGISSNGLSTMNNINGINNFSLFPRLYPVYSNLLSGSSLPHPMLN-----PASLPSSLPTDGARRLL 321
Cdd:COG5048   99 PLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSssvntPQSNSLHPPLPANSLSK 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 322 PPEHPKEVLIPAPHSAFSLTGAAASMKDESSPPSGSptagtaatSEHVVQPKATSSVMAAPSTDGAMNLIKNKRNMTGYK 401
Cdd:COG5048  179 DPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSS--------SSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 402 TLPYPlkkqNGKIKYECNVCAKTFGQLSNLKVHLRVHSGER-PFKCQTCNKGFTQLAHLQKHY--LVHTGE--KPHEC-- 474
Cdd:COG5048  251 SDSSS----SASESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpy 326
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568964813 475 QVCHKRFSSTSNLKTHLRLHSGEKPYQCK--VCPAKFTQFVHLKLHKRLHTRERPHK 529
Cdd:COG5048  327 SLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKDLKN 383
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
1-42 2.40e-04

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: 41.51  E-value: 2.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWY 42
Cdd:cd19190   81 LRFVHEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELLIGY 122
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
472-494 2.73e-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: 2.73e-04
                          10        20
                  ....*....|....*....|...
gi 568964813  472 HECQVCHKRFSSTSNLKTHLRLH 494
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
416-438 1.12e-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: 1.12e-03
                          10        20
                  ....*....|....*....|...
gi 568964813  416 YECNVCAKTFGQLSNLKVHLRVH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
444-466 1.25e-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: 1.25e-03
                          10        20
                  ....*....|....*....|...
gi 568964813  444 FKCQTCNKGFTQLAHLQKHYLVH 466
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
357-519 1.43e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 357 SPTAGTAATSEHVVQPKaTSSVMAAPSTDGAMNLIKNKRNMTGYKTLPYPLKKQNGKIKYECNVCAKTFGqlSNLKVhlr 436
Cdd:COG5189  271 SPSQGSAELFEESSLGF-DYEFIHKSVGNKEIRGGISTGEMIDVRKLPCTNSSSNGKLAHGGERNIDTPS--RMLKV--- 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964813 437 vhSGERPFKCQT--CNKGFTQLAHLQKHYLvhtgeKPHECQVCHKRFSSTSnlktHLRLHSGEKPYQCKVCPAKFTQFVH 514
Cdd:COG5189  345 --KDGKPYKCPVegCNKKYKNQNGLKYHML-----HGHQNQKLHENPSPEK----MNIFSAKDKPYRCEVCDKRYKNLNG 413

                 ....*
gi 568964813 515 LKLHK 519
Cdd:COG5189  414 LKYHR 418
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
1-41 2.49e-03

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: 38.17  E-value: 2.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568964813   1 MRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVW 41
Cdd:cd10520   75 MRFACRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLW 115
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
442-494 4.34e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.38  E-value: 4.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568964813 442 RPFkCQTCNKGFTQLAHLQ-----KHYlvhtgekphECQVCHKRFSSTSNLKTH-LRLH 494
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIqhqkaKHF---------KCHICHKKLYTAGGLAVHcLQVH 49
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
442-495 6.46e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 6.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568964813 442 RPFKCQTCNKGFTQLAHLQKHYLVHTGEKPHECQV--CHKRFSSTSNLKTHLRLHS 495
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHH 87
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
472-497 6.49e-03

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 34.53  E-value: 6.49e-03
                          10        20
                  ....*....|....*....|....*.
gi 568964813  472 HECQVCHKRFSSTSNLKTHLRLHSGE 497
Cdd:pfam13912   2 HECSECGKSFPSYQALGGHKKSHRKE 27
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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