NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|66774229|sp|Q06732|]
View 

RecName: Full=Zinc finger protein 33B; AltName: Full=Zinc finger protein 11B; AltName: Full=Zinc finger protein KOX2

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204794)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-71 4.22e-36

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 130.02  E-value: 4.22e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229     12 VSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVGYCAHKPEVIFRLEQGEEPW 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
383-772 3.73e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 383 KPFECNECGKAFSHKSALTLHQRTHTGEKPYQCNA--CGKTFYQKSDLTKHQRTHTGQKPYEC------YECGKSFCMNS 454
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplSNSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 455 HLTVHQRTHtgekpfeCLECGKSFCQKSHLTQH----QRTHIGDKPYECNACGKTFYHKSVLTRHQIIHTGLKPYECYEc 530
Cdd:COG5048 112 SSSSNSNDN-------NLLSSHSLPPSSRDPQLpdllSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSN- 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 531 gktfclkSDLTIHQRTHTGEKPFACPECGKFFSHKSTLSQHYRTHTGEKPYECHECGKIF------YNKSYLTKHNRTHT 604
Cdd:COG5048 184 -------LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSS 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 605 GEKPYECNECGKTFCQKSQLTQHQRIHIG-EKPYECNECGKAFCHKSALIVHQRT--HTQE--KPYKCNE--CGKSFCVK 677
Cdd:COG5048 257 ASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 678 SGLILHERKHTGEKPYECNECGKSFSHKSSLTVHHRA---------HTGEKSCQCNECGKIFYRKSDLAKHQRSHTGEKP 748
Cdd:COG5048 337 DALKRHILLHTSISPAKEKLLNSSSKFSPLLNNEPPQslqqykdlkNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRP 416

                       410       420
                ....*....|....*....|....*.
gi 66774229 749 YECN--TCRKTFSQKSNLIVHQRTHI 772
Cdd:COG5048 417 YNCKnpPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
343-367 3.54e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*
gi 66774229   343 HLTRHQRVHTGEKHFQCNQCGKTFW 367
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-71 4.22e-36

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 130.02  E-value: 4.22e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229     12 VSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVGYCAHKPEVIFRLEQGEEPW 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 1.25e-24

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: 96.77  E-value: 1.25e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 66774229    11 SVSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-50 1.17e-20

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: 85.29  E-value: 1.17e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 66774229  12 VSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVS 50
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
383-772 3.73e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 383 KPFECNECGKAFSHKSALTLHQRTHTGEKPYQCNA--CGKTFYQKSDLTKHQRTHTGQKPYEC------YECGKSFCMNS 454
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplSNSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 455 HLTVHQRTHtgekpfeCLECGKSFCQKSHLTQH----QRTHIGDKPYECNACGKTFYHKSVLTRHQIIHTGLKPYECYEc 530
Cdd:COG5048 112 SSSSNSNDN-------NLLSSHSLPPSSRDPQLpdllSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSN- 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 531 gktfclkSDLTIHQRTHTGEKPFACPECGKFFSHKSTLSQHYRTHTGEKPYECHECGKIF------YNKSYLTKHNRTHT 604
Cdd:COG5048 184 -------LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSS 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 605 GEKPYECNECGKTFCQKSQLTQHQRIHIG-EKPYECNECGKAFCHKSALIVHQRT--HTQE--KPYKCNE--CGKSFCVK 677
Cdd:COG5048 257 ASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 678 SGLILHERKHTGEKPYECNECGKSFSHKSSLTVHHRA---------HTGEKSCQCNECGKIFYRKSDLAKHQRSHTGEKP 748
Cdd:COG5048 337 DALKRHILLHTSISPAKEKLLNSSSKFSPLLNNEPPQslqqykdlkNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRP 416

                       410       420
                ....*....|....*....|....*.
gi 66774229 749 YECN--TCRKTFSQKSNLIVHQRTHI 772
Cdd:COG5048 417 YNCKnpPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
371-396 4.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.46e-04
                          10        20
                  ....*....|....*....|....*.
gi 66774229   371 NLTKHQRSHTGEKPFECNECGKAFSH 396
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
343-367 3.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*
gi 66774229   343 HLTRHQRVHTGEKHFQCNQCGKTFW 367
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 467-515 5.02e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.77  E-value: 5.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66774229 467 KPFeCLECGKSFCQKSHLTQHQRThigdKPYECNACGKTFYHKSVLTRH 515
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVH 44
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 327-375 9.69e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 9.69e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66774229 327 KHFeCNECGKAFWEKSHLTRHQRvhtgEKHFQCNQCGKTFWEKSNLTKH 375
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-71 4.22e-36

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 130.02  E-value: 4.22e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229     12 VSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVGYCAHKPEVIFRLEQGEEPW 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 1.25e-24

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: 96.77  E-value: 1.25e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 66774229    11 SVSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-50 1.17e-20

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: 85.29  E-value: 1.17e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 66774229  12 VSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVS 50
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
383-772 3.73e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 383 KPFECNECGKAFSHKSALTLHQRTHTGEKPYQCNA--CGKTFYQKSDLTKHQRTHTGQKPYEC------YECGKSFCMNS 454
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplSNSKASSSSLS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 455 HLTVHQRTHtgekpfeCLECGKSFCQKSHLTQH----QRTHIGDKPYECNACGKTFYHKSVLTRHQIIHTGLKPYECYEc 530
Cdd:COG5048 112 SSSSNSNDN-------NLLSSHSLPPSSRDPQLpdllSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSN- 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 531 gktfclkSDLTIHQRTHTGEKPFACPECGKFFSHKSTLSQHYRTHTGEKPYECHECGKIF------YNKSYLTKHNRTHT 604
Cdd:COG5048 184 -------LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSS 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 605 GEKPYECNECGKTFCQKSQLTQHQRIHIG-EKPYECNECGKAFCHKSALIVHQRT--HTQE--KPYKCNE--CGKSFCVK 677
Cdd:COG5048 257 ASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 678 SGLILHERKHTGEKPYECNECGKSFSHKSSLTVHHRA---------HTGEKSCQCNECGKIFYRKSDLAKHQRSHTGEKP 748
Cdd:COG5048 337 DALKRHILLHTSISPAKEKLLNSSSKFSPLLNNEPPQslqqykdlkNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRP 416

                       410       420
                ....*....|....*....|....*.
gi 66774229 749 YECN--TCRKTFSQKSNLIVHQRTHI 772
Cdd:COG5048 417 YNCKnpPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
329-674 9.56e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.64  E-value: 9.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 329 FECNECGKAFWEKSHLTRHQRVHTGEKHFQCNQ--CGKTFWEKSNLTKHQRSHTGEKPFEC----------------NEC 390
Cdd:COG5048  34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSSS 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 391 GKAFSHKSALTLHQRTHTGEKPYQCNACGKTFYQKSDLTKHQRTHTGQK-------PYECYECGKSFCMNSHLTVHQRTH 463
Cdd:COG5048 114 SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPqsnslhpPLPANSLSKDPSSNLSLLISSNVS 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 464 TGEKPFECLECGKSFCQKSHLTQHQRTHIGDKPYECNACG------------------------KTFYHKSVLTRHQIIH 519
Cdd:COG5048 194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSqlspksllsqspsslsssdssssaSESPRSSLPTASSQSS 273

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 520 TG-----------LKPYECYECGKTFCLKSDLTIHQRT--HTGE--KPFACPE--CGKFFSHKSTLSQHYRTHTGEKPYE 582
Cdd:COG5048 274 SPnesdsssekgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 583 CHECGKIFYNKSYLTK-------HNRTHTGEKPYEC--NECGKTFCQKSQLTQHQRIHIGEKPYECN--ECGKAFCHKSA 651
Cdd:COG5048 354 EKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYN 433

                       410       420
                ....*....|....*....|...
gi 66774229 652 LIVHQRTHTQEKPYKCNECGKSF 674
Cdd:COG5048 434 LIPHKKIHTNHAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
438-771 2.02e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 2.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 438 QKPYECYECGKSFCMNSHLTVHQRTHTGEKPFECL--ECGKSFCQKSHLTQHQRTHIGDKPYECNacgKTFYHKSVLTRH 515
Cdd:COG5048  31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASS 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 516 QIIHtglkpyecyECGKTFCLKSDLTIHQRTHTGEKPFACPECGKFFSHKSTLSQHYRTHTGEK-------PYECHECGK 588
Cdd:COG5048 108 SSLS---------SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPqsnslhpPLPANSLSK 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 589 IFYNKSYLTKHNRTHTGEKPYECNECGKTFCQKSQLTQHQRIHIGEKPYECNECGkAFCHKSAL-------IVHQRTHTQ 661
Cdd:COG5048 179 DPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNS-QLSPKSLLsqspsslSSSDSSSSA 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 662 EKPYKCNECGKSFCVKSGLILHERKHTG-EKPYECNECGKSFSHKSSLTVHHRA--HTGE--KSCQCNE--CGKIFYRKS 734
Cdd:COG5048 258 SESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRND 337

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 66774229 735 DLAKHQRSHTGEKPYEC--NTCRKTFSQKSNLIVHQRTH 771
Cdd:COG5048 338 ALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
198-618 7.33e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 7.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 198 NTLSHRENTLQHEKIQTLDHNFEYSI----CQETLLEKAVFNTRKRENAEENNCDYNEFGRTFCDSSSLLFHQIP----- 268
Cdd:COG5048  11 SNNSVLSSTPKSTLKSLSNAPRPDSCpnctDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRThhnnp 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 269 ------PSKDSHYEFSDCEKFLCvKSTLSKHDGvPVKHYDCGESGNNFRRKLCLSqlqkgdkgeKHFECNECgkafwEKS 342
Cdd:COG5048  91 sdlnskSLPLSNSKASSSSLSSS-SSNSNDNNL-LSSHSLPPSSRDPQLPDLLSI---------SNLRNNPL-----PGN 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 343 HLTRHQRVHTGEKHFQCNQ--CGKTFWEKSNLTKHQRSHTGEKPFECNECGKAFSHKSALTLHQRTHTGEKPYQCNACGK 420
Cdd:COG5048 155 NSSSVNTPQSNSLHPPLPAnsLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQ 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 421 TF------YQKSDLTKHQRTHTGQKPYECYECGKSFCMNSHLTVHQRTHTG-EKPFECLECGKSFCQKSHLTQHQRTHI- 492
Cdd:COG5048 235 LSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSVNh 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66774229 493 ---GDKPYEC--NACGKTFYHKSVLTRHQIIHTGLKPYECYEC-------GKTFCLKSDLTIHQRTHTGEKPFAC--PEC 558
Cdd:COG5048 315 sgeSLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSC 394

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66774229 559 GKFFSHKSTLSQHYRTHTGEKPYECH--ECGKIFYNKSYLTKHNRTHTGEKPYECNECGKTF 618
Cdd:COG5048 395 IRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
371-396 4.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.46e-04
                          10        20
                  ....*....|....*....|....*.
gi 66774229   371 NLTKHQRSHTGEKPFECNECGKAFSH 396
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
427-450 2.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.01e-03
                          10        20
                  ....*....|....*....|....
gi 66774229   427 DLTKHQRTHTGQKPYECYECGKSF 450
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
680-704 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 66774229   680 LILHERKHTGEKPYECNECGKSFSH 704
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
539-564 2.77e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.77e-03
                          10        20
                  ....*....|....*....|....*.
gi 66774229   539 DLTIHQRTHTGEKPFACPECGKFFSH 564
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
661-720 2.85e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 2.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66774229 661 QEKPYKCNECGKSFCVKSGLILHERKHTGEKPYECN--ECGKSFSHKSSLTVHHRAHTGEKS 720
Cdd:COG5048  30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS 91
zf-H2C2_2 pfam13465
Zinc-finger double domain;
455-478 3.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.24e-03
                          10        20
                  ....*....|....*....|....
gi 66774229   455 HLTVHQRTHTGEKPFECLECGKSF 478
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
651-674 3.37e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.37e-03
                          10        20
                  ....*....|....*....|....
gi 66774229   651 ALIVHQRTHTQEKPYKCNECGKSF 674
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
343-367 3.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*
gi 66774229   343 HLTRHQRVHTGEKHFQCNQCGKTFW 367
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
735-760 3.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.76e-03
                          10        20
                  ....*....|....*....|....*.
gi 66774229   735 DLAKHQRSHTGEKPYECNTCRKTFSQ 760
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
595-618 4.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.58e-03
                          10        20
                  ....*....|....*....|....
gi 66774229   595 YLTKHNRTHTGEKPYECNECGKTF 618
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
624-646 5.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.00e-03
                          10        20
                  ....*....|....*....|...
gi 66774229   624 LTQHQRIHIGEKPYECNECGKAF 646
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 467-515 5.02e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.77  E-value: 5.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66774229 467 KPFeCLECGKSFCQKSHLTQHQRThigdKPYECNACGKTFYHKSVLTRH 515
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 609-631 5.07e-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: 5.07e-03
                          10        20
                  ....*....|....*....|...
gi 66774229   609 YECNECGKTFCQKSQLTQHQRIH 631
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 469-491 5.48e-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: 5.48e-03
                          10        20
                  ....*....|....*....|...
gi 66774229   469 FECLECGKSFCQKSHLTQHQRTH 491
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
568-590 7.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 7.33e-03
                          10        20
                  ....*....|....*....|...
gi 66774229   568 LSQHYRTHTGEKPYECHECGKIF 590
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
399-424 7.63e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 7.63e-03
                          10        20
                  ....*....|....*....|....*.
gi 66774229   399 ALTLHQRTHTGEKPYQCNACGKTFYQ 424
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 385-407 8.20e-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: 34.58  E-value: 8.20e-03
                          10        20
                  ....*....|....*....|...
gi 66774229   385 FECNECGKAFSHKSALTLHQRTH 407
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 413-435 8.53e-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: 8.53e-03
                          10        20
                  ....*....|....*....|...
gi 66774229   413 YQCNACGKTFYQKSDLTKHQRTH 435
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-508 9.56e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 9.56e-03
                          10        20
                  ....*....|....*....|....*.
gi 66774229   483 HLTQHQRTHIGDKPYECNACGKTFYH 508
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 635-683 9.59e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 9.59e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66774229 635 KPYeCNECGKAFCHKSALIVHQRTHTqekpYKCNECGKSFCVKSGLILH 683
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 327-375 9.69e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 9.69e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66774229 327 KHFeCNECGKAFWEKSHLTRHQRvhtgEKHFQCNQCGKTFWEKSNLTKH 375
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVH 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH