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Conserved domains on  [gi|24582348|ref|NP_723223|]
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senseless-2, isoform A [Drosophila melanogaster]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 15210886)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation; similar to Saccharomyces cerevisiae zinc-responsive transcriptional regulator ZAP1 that controls zinc-responsive gene expression

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940|10940247|12665246|11179890
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
606-631 1.32e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.32e-05
                          10        20
                  ....*....|....*....|....*.
gi 24582348   606 DMKKHTYIHTGEKPHKCQVCGKAFSQ 631
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like super family cl41227
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 534-589 3.25e-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.


The actual alignment was detected with superfamily member cd20908:

Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 42.93  E-value: 3.25e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582348 534 KPYaCELCNKTFGHEVSLSQH-RAVHnvekvFECKQCGKRFKRSSTLSTHLL-IHSDT 589
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHqKAKH-----FKCHICHKKLYTAGGLAVHCLqVHKET 52
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
504-672 1.66e-04

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 504 SDLYSCMKCEKMFSTPHGLEVHSRRTHHGKKPYACELCNKTFGHEVSLSQHR--AVHNVE--KVFEC--KQCGKRFKRSS 577
Cdd:COG5048 258 SESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRND 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 578 TLSTHLLIHSDTRPYPCNY--CGKRFHQKSDMKKHTYIHTGEKPHKCQV-------CGKAFSQSSNLITHSRKHTGYKP- 647
Cdd:COG5048 338 ALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQQYKDLKNDKKsetlsnsCIRNFKRDSNLSLHIITHLSFRPy 417

                       170       180
                ....*....|....*....|....*.
gi 24582348 648 -FSCKLCHKAFQRKVDLRRHKETQHT 672
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTN 443
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
606-631 1.32e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.32e-05
                          10        20
                  ....*....|....*....|....*.
gi 24582348   606 DMKKHTYIHTGEKPHKCQVCGKAFSQ 631
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 534-589 3.25e-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: 42.93  E-value: 3.25e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582348 534 KPYaCELCNKTFGHEVSLSQH-RAVHnvekvFECKQCGKRFKRSSTLSTHLL-IHSDT 589
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHqKAKH-----FKCHICHKKLYTAGGLAVHCLqVHKET 52
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
504-672 1.66e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 504 SDLYSCMKCEKMFSTPHGLEVHSRRTHHGKKPYACELCNKTFGHEVSLSQHR--AVHNVE--KVFEC--KQCGKRFKRSS 577
Cdd:COG5048 258 SESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRND 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 578 TLSTHLLIHSDTRPYPCNY--CGKRFHQKSDMKKHTYIHTGEKPHKCQV-------CGKAFSQSSNLITHSRKHTGYKP- 647
Cdd:COG5048 338 ALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQQYKDLKNDKKsetlsnsCIRNFKRDSNLSLHIITHLSFRPy 417

                       170       180
                ....*....|....*....|....*.
gi 24582348 648 -FSCKLCHKAFQRKVDLRRHKETQHT 672
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTN 443
zf-H2C2_2 pfam13465
Zinc-finger double domain;
634-657 5.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.21e-04
                          10        20
                  ....*....|....*....|....
gi 24582348   634 NLITHSRKHTGYKPFSCKLCHKAF 657
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 564-586 8.00e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 8.00e-04
                          10        20
                  ....*....|....*....|...
gi 24582348   564 FECKQCGKRFKRSSTLSTHLLIH 586
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
606-631 1.32e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.32e-05
                          10        20
                  ....*....|....*....|....*.
gi 24582348   606 DMKKHTYIHTGEKPHKCQVCGKAFSQ 631
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 534-589 3.25e-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: 42.93  E-value: 3.25e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582348 534 KPYaCELCNKTFGHEVSLSQH-RAVHnvekvFECKQCGKRFKRSSTLSTHLL-IHSDT 589
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHqKAKH-----FKCHICHKKLYTAGGLAVHCLqVHKET 52
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
504-672 1.66e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 504 SDLYSCMKCEKMFSTPHGLEVHSRRTHHGKKPYACELCNKTFGHEVSLSQHR--AVHNVE--KVFEC--KQCGKRFKRSS 577
Cdd:COG5048 258 SESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRND 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 578 TLSTHLLIHSDTRPYPCNY--CGKRFHQKSDMKKHTYIHTGEKPHKCQV-------CGKAFSQSSNLITHSRKHTGYKP- 647
Cdd:COG5048 338 ALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQQYKDLKNDKKsetlsnsCIRNFKRDSNLSLHIITHLSFRPy 417

                       170       180
                ....*....|....*....|....*.
gi 24582348 648 -FSCKLCHKAFQRKVDLRRHKETQHT 672
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTN 443
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
574-668 1.95e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 574 KRSSTLSTHLLIHSDTRPYPCNYCGKRFHQKSDMKKHTYIHTGEKPHKCQV--CGKAFSQSSNLITHSRKHTGYKPFSck 651
Cdd:COG5048  16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDL-- 93

                        90
                ....*....|....*..
gi 24582348 652 LCHKAFQRKVDLRRHKE 668
Cdd:COG5048  94 NSKSLPLSNSKASSSSL 110
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 620-642 4.44e-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: 4.44e-04
                          10        20
                  ....*....|....*....|...
gi 24582348   620 HKCQVCGKAFSQSSNLITHSRKH 642
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
634-657 5.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.21e-04
                          10        20
                  ....*....|....*....|....
gi 24582348   634 NLITHSRKHTGYKPFSCKLCHKAF 657
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 564-586 8.00e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 8.00e-04
                          10        20
                  ....*....|....*....|...
gi 24582348   564 FECKQCGKRFKRSSTLSTHLLIH 586
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
550-575 2.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.02e-03
                          10        20
                  ....*....|....*....|....*.
gi 24582348   550 SLSQHRAVHNVEKVFECKQCGKRFKR 575
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 592-614 4.72e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.72e-03
                          10        20
                  ....*....|....*....|...
gi 24582348   592 YPCNYCGKRFHQKSDMKKHTYIH 614
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 561-643 8.74e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.32  E-value: 8.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582348 561 EKVFECK--QCGKRFKRSSTLSTHLLiHSdtrpypcnYCGKRFHQKSDMKKHTYIHTGEKPHKCQVCGKAFSQSSNLITH 638
Cdd:COG5189 347 GKPYKCPveGCNKKYKNQNGLKYHML-HG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417


                ....*
gi 24582348 639 sRKHT 643
Cdd:COG5189 418 -RKHS 421
 
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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