NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1917203534|ref|NP_001375099|]
View 

zinc finger protein 226 isoform a [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 16102482)

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

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0005515|GO:0008270|GO:0003677|GO:0006355|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

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;
8-67 7.87e-24

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 7.87e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203534    8 VTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLSVGHPPFKQDV-SPIERNEQLWI 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLiSQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
359-774 1.02e-19

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.22  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 359 AEKPYNCEECGRAFSQASHLQDHQRLHTGEKPFKCDA--CGKSFSRNSHLQSHQRVHTGEKPYKCEECGKG--FICSSNL 434
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 435 YIHQRVHTgEKPYKCEECGKGFS---------------RPSSLQAHQGVHTGEKSYICT-------VCGKGFTLSSNLQA 492
Cdd:COG5048   110 LSSSSSNS-NDNNLLSSHSLPPSsrdpqlpdllsisnlRNNPLPGNNSSSVNTPQSNSLhpplpanSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 493 HQRVHTGEKPYKCNECGKSFRRNSHYQVHLVVHTGEKPYKCEICGKGFSQSSYLQIHQKAHSIEKPFKCEECGQGFNQSS 572
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 573 RLQIHQLIHTGE-------KPYKCEECGKGFSRRADLKIH--CRIHTGEkpynceecgkvfrqasNLLAHQRVHSGekpf 643
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHlrSVNHSGE----------------SLKPFSCPYSL---- 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 644 kceeCGKSFGRSAHLQAHQKVHTGDKPYKC--DECGKGFKWSLN----LDMHQRVHTGEKPYKCG---ECGKYFSQASSL 714
Cdd:COG5048   329 ----CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppQSLQQYKDLKNDKKSETlsnSCIRNFKRDSNL 404

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917203534 715 QLHQSVHTGEKP--YKCDVCGKVFSRSSQLQSHQRVHTGEKPYKCEICGKSFswRSNLTVHH 774
Cdd:COG5048   405 SLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR--RDLDLSNH 464
SUF4-like super family cl41227
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 306-357 1.14e-04

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


The actual alignment was detected with superfamily member cd20908:

Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 41.39  E-value: 1.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1917203534 306 KLKCDECGKEFSQGAHLQTHQKvhviEKPYKCKQCGKGFSRRSALNVHCK-VH 357
Cdd:cd20908     1 KPWCYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLqVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 7.87e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 7.87e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203534    8 VTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLSVGHPPFKQDV-SPIERNEQLWI 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLiSQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 8-48 1.49e-20

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: 85.21  E-value: 1.49e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1917203534   8 VTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLSVG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
359-774 1.02e-19

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.22  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 359 AEKPYNCEECGRAFSQASHLQDHQRLHTGEKPFKCDA--CGKSFSRNSHLQSHQRVHTGEKPYKCEECGKG--FICSSNL 434
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 435 YIHQRVHTgEKPYKCEECGKGFS---------------RPSSLQAHQGVHTGEKSYICT-------VCGKGFTLSSNLQA 492
Cdd:COG5048   110 LSSSSSNS-NDNNLLSSHSLPPSsrdpqlpdllsisnlRNNPLPGNNSSSVNTPQSNSLhpplpanSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 493 HQRVHTGEKPYKCNECGKSFRRNSHYQVHLVVHTGEKPYKCEICGKGFSQSSYLQIHQKAHSIEKPFKCEECGQGFNQSS 572
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 573 RLQIHQLIHTGE-------KPYKCEECGKGFSRRADLKIH--CRIHTGEkpynceecgkvfrqasNLLAHQRVHSGekpf 643
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHlrSVNHSGE----------------SLKPFSCPYSL---- 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 644 kceeCGKSFGRSAHLQAHQKVHTGDKPYKC--DECGKGFKWSLN----LDMHQRVHTGEKPYKCG---ECGKYFSQASSL 714
Cdd:COG5048   329 ----CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppQSLQQYKDLKNDKKSETlsnSCIRNFKRDSNL 404

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917203534 715 QLHQSVHTGEKP--YKCDVCGKVFSRSSQLQSHQRVHTGEKPYKCEICGKSFswRSNLTVHH 774
Cdd:COG5048   405 SLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR--RDLDLSNH 464
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 3.76e-16

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: 72.58  E-value: 3.76e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1917203534   8 VTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLS 46
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 306-357 1.14e-04

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: 41.39  E-value: 1.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1917203534 306 KLKCDECGKEFSQGAHLQTHQKvhviEKPYKCKQCGKGFSRRSALNVHCK-VH 357
Cdd:cd20908     1 KPWCYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLqVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
489-514 1.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 489 NLQAHQRVHTGEKPYKCNECGKSFRR 514
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 361-413 1.93e-04

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: 40.62  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1917203534 361 KPYnCEECGRAFSQASHLQDHQRLHTgekpFKCDACGKSFSRNSHLQSH-QRVH 413
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 7.87e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 7.87e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203534    8 VTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLSVGHPPFKQDV-SPIERNEQLWI 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLiSQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 8-48 1.49e-20

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: 85.21  E-value: 1.49e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1917203534   8 VTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLSVG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
359-774 1.02e-19

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 93.22  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 359 AEKPYNCEECGRAFSQASHLQDHQRLHTGEKPFKCDA--CGKSFSRNSHLQSHQRVHTGEKPYKCEECGKG--FICSSNL 434
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 435 YIHQRVHTgEKPYKCEECGKGFS---------------RPSSLQAHQGVHTGEKSYICT-------VCGKGFTLSSNLQA 492
Cdd:COG5048   110 LSSSSSNS-NDNNLLSSHSLPPSsrdpqlpdllsisnlRNNPLPGNNSSSVNTPQSNSLhpplpanSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 493 HQRVHTGEKPYKCNECGKSFRRNSHYQVHLVVHTGEKPYKCEICGKGFSQSSYLQIHQKAHSIEKPFKCEECGQGFNQSS 572
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 573 RLQIHQLIHTGE-------KPYKCEECGKGFSRRADLKIH--CRIHTGEkpynceecgkvfrqasNLLAHQRVHSGekpf 643
Cdd:COG5048   269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHlrSVNHSGE----------------SLKPFSCPYSL---- 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 644 kceeCGKSFGRSAHLQAHQKVHTGDKPYKC--DECGKGFKWSLN----LDMHQRVHTGEKPYKCG---ECGKYFSQASSL 714
Cdd:COG5048   329 ----CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppQSLQQYKDLKNDKKSETlsnSCIRNFKRDSNL 404

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917203534 715 QLHQSVHTGEKP--YKCDVCGKVFSRSSQLQSHQRVHTGEKPYKCEICGKSFswRSNLTVHH 774
Cdd:COG5048   405 SLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR--RDLDLSNH 464
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 3.76e-16

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: 72.58  E-value: 3.76e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1917203534   8 VTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLS 46
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
245-628 4.23e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 4.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 245 IHTGQKSYQCN--ECKKPFSDLSSFDLHQQLQSGEKSLTCverGKGFCYSPVLPVHQKV---HVGEKLKCDECGKEFSQG 319
Cdd:COG5048    55 SHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLN---SKSLPLSNSKASSSSLsssSSNSNDNNLLSSHSLPPS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 320 AHLQTHQKVHVIEKPYKCKQCGKGFSRRSALNVHCKVHTAEKPYNCEECGRAFSQASHLqdhqRLHTGEKPFKCDACGKS 399
Cdd:COG5048   132 SRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISS----NVSTSIPSSSENSPLSS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 400 FSRNSHLQSHQRVHTGEKPYKCEECGKGFICSSNLYIHQRVHTGEKPYKCEECGKGFSRPSSLQAHQGVHTGE------- 472
Cdd:COG5048   208 SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfs 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 473 KSYICTVCGKGFTLSSNLQAHQR--VHTGE--KPYKCNE--CGKSFRRNSHYQVHLVVHTGEKPYKC--EICGKGFSQSS 544
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 545 Y---LQIHQKAHSIE--KPFKCEECGQGFNQSSR----LQIHQLIHTGEKPYKCEECGKGFSRRADLKIHCRIHTGEKPY 615
Cdd:COG5048   368 NnepPQSLQQYKDLKndKKSETLSNSCIRNFKRDsnlsLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                         410
                  ....*....|...
gi 1917203534 616 NCEECGKVFRQAS 628
Cdd:COG5048   448 LCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
473-799 8.48e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 8.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 473 KSYICTVCGKGFTLSSNLQAHQRVHTGEKPYKCN--ECGKSFRRNSHYQVHLVVHTGEKPYKCEicgKGFSQSSYLQIHQ 550
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 551 K-AHSIEKPFKCE-ECGQGFNQSSRLQIHQLIHTGEKPYKCEECGKGFSRRADLKIHCRIHTGEKPYNCEECGKvfrqAS 628
Cdd:COG5048   109 SlSSSSSNSNDNNlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSS----NL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 629 NLLAHQRVHSGEKPFKCEECGKSFGRSAHLQAHQKVHTGDKPYKCDECGKGFK------WSLNLDMHQRVHTGEKPYKCG 702
Cdd:COG5048   185 SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPksllsqSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 703 ECGKYFSQASSLQLHQSVHTG-EKPYKCDVCGKVFSRSSQLQSHQR--VHTGE--KPYKC--EICGKSFSWRSNLTVHHR 775
Cdd:COG5048   265 LPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                         330       340
                  ....*....|....*....|....*..
gi 1917203534 776 IHVGDKSYK---SNRGGKNIRESTQEK 799
Cdd:COG5048   345 LHTSISPAKeklLNSSSKFSPLLNNEP 371
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
241-516 3.54e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 241 HNSMIHTGQKSYQCNECKKPFSDLSSFDLHQQlqsgEKSLTCVERGK-GFCYSPVLPVHQKVHVGEKL---KCDECGKEF 316
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNL----ENSSSSLPLTTnSQLSPKSLLSQSPSSLSSSDsssSASESPRSS 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 317 SQGAHLQTHQKVHV-------IEKPYKCKQCGKGFSRRSALNVH--CKVHTAE--KPYNCEE--CGRAFSQASHLQDHQR 383
Cdd:COG5048   265 LPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 384 LHTGEKPFKCDA--CGKSFSRNSHLQSHQRVHtgekPYKCEECGKGFICSSNLYIhqrvhtgekpykceecgKGFSRPSS 461
Cdd:COG5048   345 LHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ----QYKDLKNDKKSETLSNSCI-----------------RNFKRDSN 403

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1917203534 462 LQAHQGVHTGEKS--YICTVCGKGFTLSSNLQAHQRVHTGEKPYKCNECGKSFRRNS 516
Cdd:COG5048   404 LSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 514-605 6.90e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.25  E-value: 6.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 514 RNSHYQVHLVVHTGEKPYKCEI--CGKGFSQSSYLQIHQK-AHsiekpfkceeCGQGFNQSSRLQIHQLIHTGEKPYKCE 590
Cdd:COG5189   333 RNIDTPSRMLKVKDGKPYKCPVegCNKKYKNQNGLKYHMLhGH----------QNQKLHENPSPEKMNIFSAKDKPYRCE 402

                          90
                  ....*....|....*
gi 1917203534 591 ECGKGFSRRADLKIH 605
Cdd:COG5189   403 VCDKRYKNLNGLKYH 417
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 306-357 1.14e-04

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: 41.39  E-value: 1.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1917203534 306 KLKCDECGKEFSQGAHLQTHQKvhviEKPYKCKQCGKGFSRRSALNVHCK-VH 357
Cdd:cd20908     1 KPWCYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLqVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
489-514 1.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 489 NLQAHQRVHTGEKPYKCNECGKSFRR 514
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
377-402 1.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 377 HLQDHQRLHTGEKPFKCDACGKSFSR 402
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
405-430 1.48e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.48e-04
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 405 HLQSHQRVHTGEKPYKCEECGKGFIC 430
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 361-413 1.93e-04

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: 40.62  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1917203534 361 KPYnCEECGRAFSQASHLQDHQRLHTgekpFKCDACGKSFSRNSHLQSH-QRVH 413
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
742-765 2.41e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.41e-04
                          10        20
                  ....*....|....*....|....
gi 1917203534 742 LQSHQRVHTGEKPYKCEICGKSFS 765
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 667-750 2.67e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.32  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203534 667 GDKPYKCD--ECGKGFKWSLNLDMHqRVHtgekpykcGECGKYFSQASSLQLHQSVHTGEKPYKCDVCGKVFSRSSQLQS 744
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1917203534 745 HqRVHT 750
Cdd:COG5189   417 H-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
685-710 4.05e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.05e-04
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 685 NLDMHQRVHTGEKPYKCGECGKYFSQ 710
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-458 4.74e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 4.74e-04
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 433 NLYIHQRVHTGEKPYKCEECGKGFSR 458
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
601-626 6.62e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.62e-04
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 601 DLKIHCRIHTGEKPYNCEECGKVFRQ 626
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
657-681 7.82e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.82e-04
                          10        20
                  ....*....|....*....|....*
gi 1917203534 657 HLQAHQKVHTGDKPYKCDECGKGFK 681
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 727-749 8.27e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 8.27e-04
                          10        20
                  ....*....|....*....|...
gi 1917203534 727 YKCDVCGKVFSRSSQLQSHQRVH 749
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
573-598 1.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.54e-03
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 573 RLQIHQLIHTGEKPYKCEECGKGFSR 598
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 529-577 1.55e-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: 37.92  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1917203534 529 KPYkCEICGKGFSQSSYLQIHQKAhsieKPFKCEECGQGFNQSSRLQIH 577
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
629-652 1.80e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|....
gi 1917203534 629 NLLAHQRVHSGEKPFKCEECGKSF 652
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 391-413 1.87e-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: 1.87e-03
                          10        20
                  ....*....|....*....|...
gi 1917203534 391 FKCDACGKSFSRNSHLQSHQRVH 413
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
713-738 3.38e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.38e-03
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 713 SLQLHQSVHTGEKPYKCDVCGKVFSR 738
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 615-637 4.01e-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: 4.01e-03
                          10        20
                  ....*....|....*....|...
gi 1917203534 615 YNCEECGKVFRQASNLLAHQRVH 637
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 725-773 4.23e-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: 4.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1917203534 725 KPYkCDVCGKVFSRSSQLQSHQRvhtgEKPYKCEICGKSFSWRSNLTVH 773
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 643-665 5.18e-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: 34.97  E-value: 5.18e-03
                          10        20
                  ....*....|....*....|...
gi 1917203534 643 FKCEECGKSFGRSAHLQAHQKVH 665
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 503-525 7.90e-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: 7.90e-03
                          10        20
                  ....*....|....*....|...
gi 1917203534 503 YKCNECGKSFRRNSHYQVHLVVH 525
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
517-542 9.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 9.21e-03
                          10        20
                  ....*....|....*....|....*.
gi 1917203534 517 HYQVHLVVHTGEKPYKCEICGKGFSQ 542
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 613-665 9.26e-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: 9.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1917203534 613 KPYnCEECGKVFRQASNLLAHQRvhsgEKPFKCEECGKSFGRSAHLQAH-QKVH 665
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
 
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