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Conserved domains on  [gi|123701554|ref|NP_033580|]
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zinc finger protein 37 isoform 2 [Mus musculus]

Protein Classification

KRAB_A-box and COG5048 domain-containing protein( domain architecture ID 12204416)

protein containing domains KRAB_A-box, COG5048, zf-H2C2_2, and zf-C2H2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
9-58 2.66e-16

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 73.40  E-value: 2.66e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 123701554     9 SDAEWEQLEPVQRDVYKDTKLENCSNPASMGNQDPKQDIVSVLE-EEEPSS 58
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEqGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
120-482 8.61e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 120 YGLLENKSLHSKHTPSekklLKSSSRGKNSNQNSDSLKKKPDTANDHRKSLSHSASDVNKDEIPTRKKCDKLPNNKLSDK 199
Cdd:COG5048   74 SRPLELSRHLRTHHNN----PSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNN 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 200 GDKNQTSKKCEKVCRHSASHTKEDKIQTgeKRKSHCRTPSKPEKAPGSGKPYECNHCGKVLSHKQGLLDHQRTHTGEKPY 279
Cdd:COG5048  150 PLPGNNSSSVNTPQSNSLHPPLPANSLS--KDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 280 ECNECGIAF------SQKSHLVVHQRTHTGEKPYECEQCGKAHGHKHALTDHLRIHTG-EKPYKCNECGKTFRHSSNLMQ 352
Cdd:COG5048  228 PLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTR 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 353 HLRS--HTGE--KPYECKE--CGKSFRYNSSLTEHVRTHTGEIPYECNECGKAFKYGSSLTK-------HMRIHTGEKPF 419
Cdd:COG5048  308 HLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKS 387

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123701554 420 EC--NECGKTFSKKSHLVIHQRTHTKEKP--YKCDECGKAFGHSSSLTYHMRTHTGDCPFECNQCGK 482
Cdd:COG5048  388 ETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
546-570 8.99e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.99e-04
                          10        20
                  ....*....|....*....|....*
gi 123701554  546 LVIHQRSHTGEKPYECIECGKAFKQ 570
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
517-541 1.01e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 123701554  517 HLIVHQRTHTGEKPFECYECGKAFN 541
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 503-525 2.54e-03

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  503 YECVECGKAFSQKSHLIVHQRTH 525
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-514 8.12e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.12e-03
                          10        20
                  ....*....|....*....|....*
gi 123701554  490 LTQHQRVHTGEKPYECVECGKAFSQ 514
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
9-58 2.66e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 73.40  E-value: 2.66e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 123701554     9 SDAEWEQLEPVQRDVYKDTKLENCSNPASMGNQDPKQDIVSVLE-EEEPSS 58
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEqGEEPWI 61
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 1-38 1.59e-08

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: 50.63  E-value: 1.59e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 123701554   1 MATSEPAEsdaEWEQLEPVQRDVYKDTKLENCSNPASM 38
Cdd:cd07765    6 VAVYFSQE---EWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
120-482 8.61e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 120 YGLLENKSLHSKHTPSekklLKSSSRGKNSNQNSDSLKKKPDTANDHRKSLSHSASDVNKDEIPTRKKCDKLPNNKLSDK 199
Cdd:COG5048   74 SRPLELSRHLRTHHNN----PSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNN 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 200 GDKNQTSKKCEKVCRHSASHTKEDKIQTgeKRKSHCRTPSKPEKAPGSGKPYECNHCGKVLSHKQGLLDHQRTHTGEKPY 279
Cdd:COG5048  150 PLPGNNSSSVNTPQSNSLHPPLPANSLS--KDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 280 ECNECGIAF------SQKSHLVVHQRTHTGEKPYECEQCGKAHGHKHALTDHLRIHTG-EKPYKCNECGKTFRHSSNLMQ 352
Cdd:COG5048  228 PLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTR 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 353 HLRS--HTGE--KPYECKE--CGKSFRYNSSLTEHVRTHTGEIPYECNECGKAFKYGSSLTK-------HMRIHTGEKPF 419
Cdd:COG5048  308 HLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKS 387

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123701554 420 EC--NECGKTFSKKSHLVIHQRTHTKEKP--YKCDECGKAFGHSSSLTYHMRTHTGDCPFECNQCGK 482
Cdd:COG5048  388 ETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-39 1.88e-06

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 44.77  E-value: 1.88e-06
                          10        20
                  ....*....|....*....|....*...
gi 123701554   12 EWEQLEPVQRDVYKDTKLENCSNPASMG 39
Cdd:pfam01352  15 EWALLDPAQRNLYRDVMLENYRNLVSLG 42
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-374 4.69e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.69e-05
                          10        20
                  ....*....|....*....|....*.
gi 123701554  349 NLMQHLRSHTGEKPYECKECGKSFRY 374
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
546-570 8.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.99e-04
                          10        20
                  ....*....|....*....|....*
gi 123701554  546 LVIHQRSHTGEKPYECIECGKAFKQ 570
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
517-541 1.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 123701554  517 HLIVHQRTHTGEKPFECYECGKAFN 541
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 417-468 2.05e-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: 37.54  E-value: 2.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 123701554 417 KPFeCNECGKTFSKKSHLVIHQRTHTkekpYKCDECGKAFGHSSSLTYHMRT 468
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 503-525 2.54e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  503 YECVECGKAFSQKSHLIVHQRTH 525
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-514 8.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.12e-03
                          10        20
                  ....*....|....*....|....*
gi 123701554  490 LTQHQRVHTGEKPYECVECGKAFSQ 514
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 501-549 8.99e-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: 35.61  E-value: 8.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 123701554 501 KPYeCVECGKAFSQKSHLIVHQRTHTgekpFECYECGKAFNAKSQLVIH 549
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
9-58 2.66e-16

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 73.40  E-value: 2.66e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 123701554     9 SDAEWEQLEPVQRDVYKDTKLENCSNPASMGNQDPKQDIVSVLE-EEEPSS 58
Cdd:smart00349  11 TQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEqGEEPWI 61
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 1-38 1.59e-08

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: 50.63  E-value: 1.59e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 123701554   1 MATSEPAEsdaEWEQLEPVQRDVYKDTKLENCSNPASM 38
Cdd:cd07765    6 VAVYFSQE---EWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
120-482 8.61e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 120 YGLLENKSLHSKHTPSekklLKSSSRGKNSNQNSDSLKKKPDTANDHRKSLSHSASDVNKDEIPTRKKCDKLPNNKLSDK 199
Cdd:COG5048   74 SRPLELSRHLRTHHNN----PSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNN 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 200 GDKNQTSKKCEKVCRHSASHTKEDKIQTgeKRKSHCRTPSKPEKAPGSGKPYECNHCGKVLSHKQGLLDHQRTHTGEKPY 279
Cdd:COG5048  150 PLPGNNSSSVNTPQSNSLHPPLPANSLS--KDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 280 ECNECGIAF------SQKSHLVVHQRTHTGEKPYECEQCGKAHGHKHALTDHLRIHTG-EKPYKCNECGKTFRHSSNLMQ 352
Cdd:COG5048  228 PLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTR 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 353 HLRS--HTGE--KPYECKE--CGKSFRYNSSLTEHVRTHTGEIPYECNECGKAFKYGSSLTK-------HMRIHTGEKPF 419
Cdd:COG5048  308 HLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKS 387

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123701554 420 EC--NECGKTFSKKSHLVIHQRTHTKEKP--YKCDECGKAFGHSSSLTYHMRTHTGDCPFECNQCGK 482
Cdd:COG5048  388 ETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
238-562 1.17e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 238 PSKPEKAPGSGKPYECNHCGKVLSHKQGLLDHQRTHTGEKPYECNECGIAFSQK--SHLVVHQRTHTGEKPYECEQCGKA 315
Cdd:COG5048   21 KSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSKSLPL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 316 HGHKHALTDHLRIHTGE-KPYKCNECGKTFRHSSNLMQHLRSHTGEKPYECKECGKSFR----YNSSLTEHVRTHTGEIP 390
Cdd:COG5048  101 SNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqSNSLHPPLPANSLSKDP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 391 YECNecgkafkygsSLTKHMRIHTGEKPFECNECGKTFSKKSHLVIHQRTHTKEKPYKCDECGKAFGHSSSLTYHMRTHT 470
Cdd:COG5048  181 SSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 471 GDCPFECNQCGKAFKQIEGLTQHQRVHTGE-------KPYECVECGKAFSQKSHLIVHQRT--HTGE--KPFECYE--CG 537
Cdd:COG5048  251 SDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCG 330

                        330       340
                 ....*....|....*....|....*
gi 123701554 538 KAFNAKSQLVIHQRSHTGEKPYECI 562
Cdd:COG5048  331 KLFSRNDALKRHILLHTSISPAKEK 355
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-39 1.88e-06

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 44.77  E-value: 1.88e-06
                          10        20
                  ....*....|....*....|....*...
gi 123701554   12 EWEQLEPVQRDVYKDTKLENCSNPASMG 39
Cdd:pfam01352  15 EWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
325-571 1.34e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 325 HLRIHTGEKPYKCNECGKTFRHSSNLMQHLRSHTGEKPYECKECGKSF------RYNSSLTEHVRTHTGEIPYECNECGK 398
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTA 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 399 AFKYGSSLTKHMRIHTG-EKPFECNECGKTFSKKSHLVIHQRT--HTKE--KPYKCDE--CGKAFGHSSSLTYHMRTHTG 471
Cdd:COG5048  269 SSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 472 DCPFEC--NQCGKAFKQI-----EGLTQHQRVHTGEKPYECV--ECGKAFSQKSHLIVHQRTHTGEKPFECY--ECGKAF 540
Cdd:COG5048  349 ISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSF 428

                        250       260       270
                 ....*....|....*....|....*....|.
gi 123701554 541 NAKSQLVIHQRSHTGEKPYECIECGKAFKQN 571
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-374 4.69e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.69e-05
                          10        20
                  ....*....|....*....|....*.
gi 123701554  349 NLMQHLRSHTGEKPYECKECGKSFRY 374
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
125-457 1.31e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 125 NKSLHSKHTPSEKKLLKSSSRGKNSNQNSDSLKKKPDTANDHRKSLSHSASDVNKDEIPTRKKCDK-------LPNNKLS 197
Cdd:COG5048   98 LPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslhppLPANSLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 198 DKGDKNQTSKKCEKVcRHSASHTKEDKIQTGEKRKSHCRTPSKPEKAPGSGKPYECNHCGK---VLSHKQGLLDHQRTHT 274
Cdd:COG5048  178 KDPSSNLSLLISSNV-STSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPkslLSQSPSSLSSSDSSSS 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 275 GEKPYECNECGIAFSQKSHLVVHQRTHTG-EKPYECEQCGKAHGHKHALTDHLR--IHTGE--KPYKCNE--CGKTFRHS 347
Cdd:COG5048  257 ASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRN 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123701554 348 SNLMQHLRSHTGEKPYECKECGKSFRYNSSLTE-------HVRTHTGEIPYEC--NECGKAFKYGSSLTKHMRIHTGEKP 418
Cdd:COG5048  337 DALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRP 416

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 123701554 419 --FECNECGKTFSKKSHLVIHQRTHTKEKPYKCDECGKAFG 457
Cdd:COG5048  417 ynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
405-430 2.30e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.30e-04
                          10        20
                  ....*....|....*....|....*.
gi 123701554  405 SLTKHMRIHTGEKPFECNECGKTFSK 430
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
321-346 5.45e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.45e-04
                          10        20
                  ....*....|....*....|....*.
gi 123701554  321 ALTDHLRIHTGEKPYKCNECGKTFRH 346
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 335-357 7.29e-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: 36.89  E-value: 7.29e-04
                          10        20
                  ....*....|....*....|...
gi 123701554  335 YKCNECGKTFRHSSNLMQHLRSH 357
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
546-570 8.99e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.99e-04
                          10        20
                  ....*....|....*....|....*
gi 123701554  546 LVIHQRSHTGEKPYECIECGKAFKQ 570
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
517-541 1.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 123701554  517 HLIVHQRTHTGEKPFECYECGKAFN 541
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-456 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....
gi 123701554  433 HLVIHQRTHTKEKPYKCDECGKAF 456
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 419-441 1.63e-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: 36.12  E-value: 1.63e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  419 FECNECGKTFSKKSHLVIHQRTH 441
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 417-468 2.05e-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: 37.54  E-value: 2.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 123701554 417 KPFeCNECGKTFSKKSHLVIHQRTHTkekpYKCDECGKAFGHSSSLTYHMRT 468
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47
zf-H2C2_2 pfam13465
Zinc-finger double domain;
377-402 2.05e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 123701554  377 SLTEHVRTHTGEIPYECNECGKAFKY 402
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 503-525 2.54e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  503 YECVECGKAFSQKSHLIVHQRTH 525
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
461-486 3.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.85e-03
                          10        20
                  ....*....|....*....|....*.
gi 123701554  461 SLTYHMRTHTGDCPFECNQCGKAFKQ 486
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 447-469 4.52e-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: 4.52e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  447 YKCDECGKAFGHSSSLTYHMRTH 469
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 363-385 4.57e-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: 4.57e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  363 YECKECGKSFRYNSSLTEHVRTH 385
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
293-315 5.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.93e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  293 HLVVHQRTHTGEKPYECEQCGKA 315
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKS 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
266-290 6.04e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.04e-03
                          10        20
                  ....*....|....*....|....*
gi 123701554  266 LLDHQRTHTGEKPYECNECGIAFSQ 290
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 279-301 6.57e-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: 34.20  E-value: 6.57e-03
                          10        20
                  ....*....|....*....|...
gi 123701554  279 YECNECGIAFSQKSHLVVHQRTH 301
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-514 8.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.12e-03
                          10        20
                  ....*....|....*....|....*
gi 123701554  490 LTQHQRVHTGEKPYECVECGKAFSQ 514
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 501-549 8.99e-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: 35.61  E-value: 8.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 123701554 501 KPYeCVECGKAFSQKSHLIVHQRTHTgekpFECYECGKAFNAKSQLVIH 549
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
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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