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Conserved domains on  [gi|161760658|ref|NP_663522|]
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zinc finger protein 189 [Mus musculus]

Protein Classification

KRAB_A-box and COG5048 domain-containing protein( domain architecture ID 11577739)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
116-506 1.12e-17

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 85.90  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 116 HTNVRKRPTSEEKCHKCEECGKRFVRKAHFIQHQRVHTGEKPFQCN--ECGKSFSRSSFVIEHQRIHTGERPYECNYCGK 193
Cdd:COG5048   20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 194 T--FSVSSTLIRHQrIHTGERPYQCNQCKQSFSQRRSLVKHQRIHTGEKPHKCSDC------GKAFSWKSHLIE------ 259
Cdd:COG5048  100 LsnSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvnTPQSNSLHPPLPanslsk 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 260 ----------HQRTHTGEKPYHCTKCKKSFSRNSLLVEHQRIHTGERPHKCGECGKAFRLSTYLIQHQKIHTGEKPFLCI 329
Cdd:COG5048  179 dpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 330 ECGKSFSRSSFLIEHQRIHTGER-------PYQCQECGKSFSQLCNLTRHQR--IHTG--DKPHKCEE--CGKAFSRSSG 396
Cdd:COG5048  259 ESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 397 LIQHQRIH-----IREKTSPFSETKESFDPNCS-LVIQQEVSPKEKSYKC--DDCGKTFSVSAHLVQHQRIHTGEKPYL- 467
Cdd:COG5048  339 LKRHILLHtsispAKEKLLNSSSKFSPLLNNEPpQSLQQYKDLKNDKKSEtlSNSCIRNFKRDSNLSLHIITHLSFRPYn 418

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 161760658 468 --CTVCGKSFSRSSFLIEHQRIHTGERPYLCRQCGKSFSQL 506
Cdd:COG5048  419 ckNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-39 3.60e-10

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: 55.25  E-value: 3.60e-10
                         10        20
                 ....*....|....*....|....*...
gi 161760658  12 EEWGYLDPAPRSLYKDVMMDSYGKLVSL 39
Cdd:cd07765   13 EEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
537-561 9.26e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.26e-04
                          10        20
                  ....*....|....*....|....*
gi 161760658  537 LIQHQRIHTGEKPYRCGKCDKSFSQ 561
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-533 3.32e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|....*.
gi 161760658  508 NLIRHQGVHTGNKPHKCEECGKAFSR 533
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
116-506 1.12e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 85.90  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 116 HTNVRKRPTSEEKCHKCEECGKRFVRKAHFIQHQRVHTGEKPFQCN--ECGKSFSRSSFVIEHQRIHTGERPYECNYCGK 193
Cdd:COG5048   20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 194 T--FSVSSTLIRHQrIHTGERPYQCNQCKQSFSQRRSLVKHQRIHTGEKPHKCSDC------GKAFSWKSHLIE------ 259
Cdd:COG5048  100 LsnSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvnTPQSNSLHPPLPanslsk 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 260 ----------HQRTHTGEKPYHCTKCKKSFSRNSLLVEHQRIHTGERPHKCGECGKAFRLSTYLIQHQKIHTGEKPFLCI 329
Cdd:COG5048  179 dpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 330 ECGKSFSRSSFLIEHQRIHTGER-------PYQCQECGKSFSQLCNLTRHQR--IHTG--DKPHKCEE--CGKAFSRSSG 396
Cdd:COG5048  259 ESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 397 LIQHQRIH-----IREKTSPFSETKESFDPNCS-LVIQQEVSPKEKSYKC--DDCGKTFSVSAHLVQHQRIHTGEKPYL- 467
Cdd:COG5048  339 LKRHILLHtsispAKEKLLNSSSKFSPLLNNEPpQSLQQYKDLKNDKKSEtlSNSCIRNFKRDSNLSLHIITHLSFRPYn 418

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 161760658 468 --CTVCGKSFSRSSFLIEHQRIHTGERPYLCRQCGKSFSQL 506
Cdd:COG5048  419 ckNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-39 3.60e-10

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: 55.25  E-value: 3.60e-10
                         10        20
                 ....*....|....*....|....*...
gi 161760658  12 EEWGYLDPAPRSLYKDVMMDSYGKLVSL 39
Cdd:cd07765   13 EEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB smart00349
krueppel associated box;
11-63 5.19e-10

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 55.29  E-value: 5.19e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161760658    11 KEEWGYLDPAPRSLYKDVMMDSYGKLVSLDVLNRNKDEEPtvkeELEKDIEPQ 63
Cdd:smart00349  12 QEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLIS----QLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-40 2.35e-08

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: 50.16  E-value: 2.35e-08
                          10        20
                  ....*....|....*....|....*....
gi 161760658   12 EEWGYLDPAPRSLYKDVMMDSYGKLVSLD 40
Cdd:pfam01352  14 EEWALLDPAQRNLYRDVMLENYRNLVSLG 42
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-393 5.54e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.54e-05
                          10        20
                  ....*....|....*....|....*.
gi 161760658  368 NLTRHQRIHTGDKPHKCEECGKAFSR 393
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
537-561 9.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.26e-04
                          10        20
                  ....*....|....*....|....*
gi 161760658  537 LIQHQRIHTGEKPYRCGKCDKSFSQ 561
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-533 3.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|....*.
gi 161760658  508 NLIRHQGVHTGNKPHKCEECGKAFSR 533
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 184-236 7.93e-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: 7.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161760658 184 RPYeCNYCGKTFSVSSTLIRHQRIHTgerpYQCNQCKQSFSQRRSLVKH-QRIH 236
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
116-506 1.12e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 85.90  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 116 HTNVRKRPTSEEKCHKCEECGKRFVRKAHFIQHQRVHTGEKPFQCN--ECGKSFSRSSFVIEHQRIHTGERPYECNYCGK 193
Cdd:COG5048   20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 194 T--FSVSSTLIRHQrIHTGERPYQCNQCKQSFSQRRSLVKHQRIHTGEKPHKCSDC------GKAFSWKSHLIE------ 259
Cdd:COG5048  100 LsnSKASSSSLSSS-SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssvnTPQSNSLHPPLPanslsk 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 260 ----------HQRTHTGEKPYHCTKCKKSFSRNSLLVEHQRIHTGERPHKCGECGKAFRLSTYLIQHQKIHTGEKPFLCI 329
Cdd:COG5048  179 dpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 330 ECGKSFSRSSFLIEHQRIHTGER-------PYQCQECGKSFSQLCNLTRHQR--IHTG--DKPHKCEE--CGKAFSRSSG 396
Cdd:COG5048  259 ESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 397 LIQHQRIH-----IREKTSPFSETKESFDPNCS-LVIQQEVSPKEKSYKC--DDCGKTFSVSAHLVQHQRIHTGEKPYL- 467
Cdd:COG5048  339 LKRHILLHtsispAKEKLLNSSSKFSPLLNNEPpQSLQQYKDLKNDKKSEtlSNSCIRNFKRDSNLSLHIITHLSFRPYn 418

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 161760658 468 --CTVCGKSFSRSSFLIEHQRIHTGERPYLCRQCGKSFSQL 506
Cdd:COG5048  419 ckNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
184-572 5.88e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 74.35  E-value: 5.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 184 RPYECNYCGKTFSVSSTLIRHQRIHTGERPYQCNQ--CKQSFSQRRSLVKHQRIHTGEKPHKCSD-CGKAFSWKSHLIEH 260
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKsLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 261 QRTHTGEKPYHCTKCKKSFSRNSLLVEHQRIHTGERPHKCGECGKAFRLStylIQHQKIHtGEKPFLCIECGKSFSRSSF 340
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNT---PQSNSLH-PPLPANSLSKDPSSNLSLL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 341 LieHQRIHTGERPYQCQECGKSFSQLCNLTRHQRIHTGDKPHKCEECGKAF-------SRSSGLIQHQRIHIREKTSPFS 413
Cdd:COG5048  188 I--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsqSPSSLSSSDSSSSASESPRSSL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 414 ETKESFDPNCSLVIQQEVSPKEKSYKCDDCGKTFSVSAHLVQHQR--IHTGE--KPYLCTV--CGKSFSRSSFLIEHQRI 487
Cdd:COG5048  266 PTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 488 HTGERPYLC--RQCGKSFSQLCNLIRHQGVHTGNKPHKCEE-------CGKAFSRNSGLIQHQRIHTGEKPY--RCGKCD 556
Cdd:COG5048  346 HTSISPAKEklLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKsetlsnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCS 425

                        410
                 ....*....|....*.
gi 161760658 557 KSFSQQRSLVNHQKIH 572
Cdd:COG5048  426 KSFNRHYNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-605 1.89e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.81  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 212 RPYQCNQCKQSFSQRRSLVKHQRIHTGEKPHKCSD--CGKAFSWKSHLIEHQRTHTGEKPYhcTKCKKSFSRNSLLVEHQ 289
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSD--LNSKSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 290 RIHtgerphkcgeCGKAFRLSTYLIQHQKIHTGEKPFLCIECGKSFSRSSFLIEHQRIHTGER-------PYQCQECGKS 362
Cdd:COG5048  110 LSS----------SSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPqsnslhpPLPANSLSKD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 363 FSQLCNLTRHQRIHTGDKPHKCeecgKAFSRSSGLIQHQRIHIREKTSPFSE--TKESFDPNCSLVIQQEVS--PKEKSY 438
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSE----NSPLSSSYSIPSSSSDQNLENSSSSLplTTNSQLSPKSLLSQSPSSlsSSDSSS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 439 KCDDCGKTFSVSAHLVQHQRIHTGE-------KPYLCTVCGKSFSRSSFLIEHQR--IHTGE--RPYLCR--QCGKSFSQ 505
Cdd:COG5048  256 SASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSR 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 506 LCNLIRHQGVHTGNKPHKC--EECGKAFSRNS-----GLIQHQRIHTGEKPYRC--GKCDKSFSQQRSLVNHQKIHAEVK 576
Cdd:COG5048  336 NDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFR 415

                        410       420
                 ....*....|....*....|....*....
gi 161760658 577 TQEIYeCDACGEAFTCQISLIQHQKLHIM 605
Cdd:COG5048  416 PYNCK-NPPCSKSFNRHYNLIPHKKIHTN 443
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-39 3.60e-10

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: 55.25  E-value: 3.60e-10
                         10        20
                 ....*....|....*....|....*...
gi 161760658  12 EEWGYLDPAPRSLYKDVMMDSYGKLVSL 39
Cdd:cd07765   13 EEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB smart00349
krueppel associated box;
11-63 5.19e-10

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 55.29  E-value: 5.19e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161760658    11 KEEWGYLDPAPRSLYKDVMMDSYGKLVSLDVLNRNKDEEPtvkeELEKDIEPQ 63
Cdd:smart00349  12 QEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLIS----QLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
156-340 3.65e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 156 KPFQCNECGKSFSRSSFVIEHQR--IHTGE--RPYEC--NYCGKTFSVSSTLIRHQRIHTGERPYQCNQCKQSFSQRRSL 229
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 230 vkhqrihtGEKPHKCSDcgkafswKSHLIEHQRTHTGEKPyhctKCKKSFSRNSLLVEHQRIHTGERPH--KCGECGKAF 307
Cdd:COG5048  368 --------NNEPPQSLQ-------QYKDLKNDKKSETLSN----SCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSF 428

                        170       180       190
                 ....*....|....*....|....*....|...
gi 161760658 308 RLSTYLIQHQKIHTGEKPFLCIECGKSFSRSSF 340
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-40 2.35e-08

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: 50.16  E-value: 2.35e-08
                          10        20
                  ....*....|....*....|....*....
gi 161760658   12 EEWGYLDPAPRSLYKDVMMDSYGKLVSLD 40
Cdd:pfam01352  14 EEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
410-502 3.17e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 410 SPFSETKESFDPNCSLVIQQEvSPKEKSYKCDDCGKTFSVSAHLVQHQRIHTGEKPYLCTV--CGKSFSRSSFLIEHQRI 487
Cdd:COG5048    7 QSSSSNNSVLSSTPKSTLKSL-SNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRT 85

                         90
                 ....*....|....*
gi 161760658 488 HTGERPYLCRQCGKS 502
Cdd:COG5048   86 HHNNPSDLNSKSLPL 100
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-393 5.54e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.54e-05
                          10        20
                  ....*....|....*....|....*.
gi 161760658  368 NLTRHQRIHTGDKPHKCEECGKAFSR 393
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 462-540 8.74e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.09  E-value: 8.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760658 462 GEKPYLCTV--CGKSFsRSSFLIEHQRIHTgerpylcrQCGKSFSQLCNLIRHQGVHTGNKPHKCEECGKAFSRNSGLIQ 539
Cdd:COG5189  346 DGKPYKCPVegCNKKY-KNQNGLKYHMLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 .
gi 161760658 540 H 540
Cdd:COG5189  417 H 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
452-477 3.24e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.24e-04
                          10        20
                  ....*....|....*....|....*.
gi 161760658  452 HLVQHQRIHTGEKPYLCTVCGKSFSR 477
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
341-365 6.83e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.83e-04
                          10        20
                  ....*....|....*....|....*
gi 161760658  341 LIEHQRIHTGERPYQCQECGKSFSQ 365
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
228-252 7.10e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.10e-04
                          10        20
                  ....*....|....*....|....*
gi 161760658  228 SLVKHQRIHTGEKPHKCSDCGKAFS 252
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
256-281 7.76e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.76e-04
                          10        20
                  ....*....|....*....|....*.
gi 161760658  256 HLIEHQRTHTGEKPYHCTKCKKSFSR 281
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
312-337 9.08e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.08e-04
                          10        20
                  ....*....|....*....|....*.
gi 161760658  312 YLIQHQKIHTGEKPFLCIECGKSFSR 337
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
537-561 9.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.26e-04
                          10        20
                  ....*....|....*....|....*
gi 161760658  537 LIQHQRIHTGEKPYRCGKCDKSFSQ 561
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
144-169 1.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|....*.
gi 161760658  144 HFIQHQRVHTGEKPFQCNECGKSFSR 169
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
481-505 2.50e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.50e-03
                          10        20
                  ....*....|....*....|....*
gi 161760658  481 LIEHQRIHTGERPYLCRQCGKSFSQ 505
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 354-376 3.24e-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: 3.24e-03
                          10        20
                  ....*....|....*....|...
gi 161760658  354 YQCQECGKSFSQLCNLTRHQRIH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 186-208 3.30e-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: 3.30e-03
                          10        20
                  ....*....|....*....|...
gi 161760658  186 YECNYCGKTFSVSSTLIRHQRIH 208
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-533 3.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|....*.
gi 161760658  508 NLIRHQGVHTGNKPHKCEECGKAFSR 533
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
285-307 3.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|...
gi 161760658  285 LVEHQRIHTGERPHKCGECGKAF 307
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
201-225 4.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.33e-03
                          10        20
                  ....*....|....*....|....*
gi 161760658  201 LIRHQRIHTGERPYQCNQCKQSFSQ 225
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
175-196 4.64e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.64e-03
                          10        20
                  ....*....|....*....|..
gi 161760658  175 EHQRIHTGERPYECNYCGKTFS 196
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 382-404 7.18e-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: 7.18e-03
                          10        20
                  ....*....|....*....|...
gi 161760658  382 HKCEECGKAFSRSSGLIQHQRIH 404
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 522-544 7.46e-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: 7.46e-03
                          10        20
                  ....*....|....*....|...
gi 161760658  522 HKCEECGKAFSRNSGLIQHQRIH 544
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 184-236 7.93e-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: 7.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 161760658 184 RPYeCNYCGKTFSVSSTLIRHQRIHTgerpYQCNQCKQSFSQRRSLVKH-QRIH 236
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 438-460 9.92e-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: 33.81  E-value: 9.92e-03
                          10        20
                  ....*....|....*....|...
gi 161760658  438 YKCDDCGKTFSVSAHLVQHQRIH 460
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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