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Conserved domains on  [gi|1622893442|ref|XP_014980510|]
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zinc finger protein 135 isoform X2 [Macaca mulatta]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204351)

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:0003677|GO:0008270|GO:0005515|GO:0006355|GO:0001217|GO:0003700
PubMed:  22803940|14519192|8183940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
26-84 5.28e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.30  E-value: 5.28e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622893442   26 VTFEDVVVDFSQEEWGQLKPAQRTLYRDVMLDTFRLLVSVGHWLPKPNVISLLEQEAEP 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-653 3.93e-18

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 87.83  E-value: 3.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 252 RPYECHECGKGFRNSSALTKHQRIHTGEKPYKCTQCGRTFNQIAP--LIQHQRTHTGEKPYECSECGKSFSFRSSFSQHE 329
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 330 RTHTGEkPYECSECGKAFRQSIHLTQH--LRIHTGEKPYQCGECGKAFSHSSSLTKHQRIHTGEkpyecHECGKAFTQIT 407
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 408 PLIQHQRTHTGEKPYECSECGKAFSQSTLLTEHRRIHTgEKPYGCNECGKTFSHSSSLSQHERTHTGEKPYECSQCGKAF 487
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 488 RQSTHLTQHQRIHTGE-------KPYECNDCGKAFSHSSSLTKHQR--IHTGE--KPYEC--NQCGRAFSQLAPLIQHQR 554
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 555 IHTGEKPYECNQCGRAFSQSSLLIE-------HQRIHTKEKPYGC--NECGKSFSHSSSLSQHERTHTGEKPYECHD--C 623
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNppC 424

                         410       420       430
                  ....*....|....*....|....*....|
gi 1622893442 624 GKSFRQSTHLTQHRRIHTGEKPYVCRDCGK 653
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 646-668 1.19e-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: 36.51  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 646 YVCRDCGKAFTHSSSLTKHQRTH 668
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
26-84 5.28e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.30  E-value: 5.28e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622893442   26 VTFEDVVVDFSQEEWGQLKPAQRTLYRDVMLDTFRLLVSVGHWLPKPNVISLLEQEAEP 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 26-66 1.43e-22

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: 90.61  E-value: 1.43e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622893442  26 VTFEDVVVDFSQEEWGQLKPAQRTLYRDVMLDTFRLLVSVG 66
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-653 3.93e-18

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 87.83  E-value: 3.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 252 RPYECHECGKGFRNSSALTKHQRIHTGEKPYKCTQCGRTFNQIAP--LIQHQRTHTGEKPYECSECGKSFSFRSSFSQHE 329
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 330 RTHTGEkPYECSECGKAFRQSIHLTQH--LRIHTGEKPYQCGECGKAFSHSSSLTKHQRIHTGEkpyecHECGKAFTQIT 407
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 408 PLIQHQRTHTGEKPYECSECGKAFSQSTLLTEHRRIHTgEKPYGCNECGKTFSHSSSLSQHERTHTGEKPYECSQCGKAF 487
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 488 RQSTHLTQHQRIHTGE-------KPYECNDCGKAFSHSSSLTKHQR--IHTGE--KPYEC--NQCGRAFSQLAPLIQHQR 554
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 555 IHTGEKPYECNQCGRAFSQSSLLIE-------HQRIHTKEKPYGC--NECGKSFSHSSSLSQHERTHTGEKPYECHD--C 623
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNppC 424

                         410       420       430
                  ....*....|....*....|....*....|
gi 1622893442 624 GKSFRQSTHLTQHRRIHTGEKPYVCRDCGK 653
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 26-64 4.18e-18

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: 77.97  E-value: 4.18e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622893442  26 VTFEDVVVDFSQEEWGQLKPAQRTLYRDVMLDTFRLLVS 64
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-405 1.32e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.32e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 380 SLTKHQRIHTGEKPYECHECGKAFTQ 405
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 646-668 1.19e-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: 36.51  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 646 YVCRDCGKAFTHSSSLTKHQRTH 668
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 532-588 7.36e-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: 7.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622893442 532 KPYeCNQCGRAFSQLAPLIQHQRIHTgekpYECNQCGRAFSQSSLLIEH-QRIHtKEK 588
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH-KET 52
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
26-84 5.28e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.30  E-value: 5.28e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622893442   26 VTFEDVVVDFSQEEWGQLKPAQRTLYRDVMLDTFRLLVSVGHWLPKPNVISLLEQEAEP 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 26-66 1.43e-22

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: 90.61  E-value: 1.43e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622893442  26 VTFEDVVVDFSQEEWGQLKPAQRTLYRDVMLDTFRLLVSVG 66
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-653 3.93e-18

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 87.83  E-value: 3.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 252 RPYECHECGKGFRNSSALTKHQRIHTGEKPYKCTQCGRTFNQIAP--LIQHQRTHTGEKPYECSECGKSFSFRSSFSQHE 329
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 330 RTHTGEkPYECSECGKAFRQSIHLTQH--LRIHTGEKPYQCGECGKAFSHSSSLTKHQRIHTGEkpyecHECGKAFTQIT 407
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 408 PLIQHQRTHTGEKPYECSECGKAFSQSTLLTEHRRIHTgEKPYGCNECGKTFSHSSSLSQHERTHTGEKPYECSQCGKAF 487
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 488 RQSTHLTQHQRIHTGE-------KPYECNDCGKAFSHSSSLTKHQR--IHTGE--KPYEC--NQCGRAFSQLAPLIQHQR 554
Cdd:COG5048   265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHIL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 555 IHTGEKPYECNQCGRAFSQSSLLIE-------HQRIHTKEKPYGC--NECGKSFSHSSSLSQHERTHTGEKPYECHD--C 623
Cdd:COG5048   345 LHTSISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNppC 424

                         410       420       430
                  ....*....|....*....|....*....|
gi 1622893442 624 GKSFRQSTHLTQHRRIHTGEKPYVCRDCGK 653
Cdd:COG5048   425 SKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 26-64 4.18e-18

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: 77.97  E-value: 4.18e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622893442  26 VTFEDVVVDFSQEEWGQLKPAQRTLYRDVMLDTFRLLVS 64
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
222-631 1.18e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 80.12  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 222 KEKPYKCQECRKAFSHSSALIEHHRTHTGERPYECH--ECGKGFRNSSALTKHQRIHTGEKPYKCTQCGRTFNQIAPLIQ 299
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 300 HQRTHTGE-KPYECSECGKSFSFRSSFSQHERTHTGEKPYECSECGKAFRQSIhltQHLRIHtGEKPYQCgECGKAFSHS 378
Cdd:COG5048   110 LSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP---QSNSLH-PPLPANS-LSKDPSSNL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 379 SSLTKHQRIHTGEKPYECHECGKaFTQITPLIQHQRTHTGEKPYECSECGKAF-------SQSTLLTEHRRIHTGEkpyg 451
Cdd:COG5048   185 SLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsqSPSSLSSSDSSSSASE---- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 452 CNECGKTFSHSSSLSQ---HERTHTG-EKPYECSQCGKAFRQSTHLTQHQR--IHTGE--KPYEC--NDCGKAFSHSSSL 521
Cdd:COG5048   260 SPRSSLPTASSQSSSPnesDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDAL 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 522 TKHQRIHTGEKPYEC--NQCGRAFSQLAP-----LIQHQRIHTGEKPYEC--NQCGRAFSQSSLLIEHQRIHTKEKPYGC 592
Cdd:COG5048   340 KRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNC 419

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1622893442 593 N--ECGKSFSHSSSLSQHERTHTGEKPYECHDCGKSFRQST 631
Cdd:COG5048   420 KnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
336-669 3.32e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.42  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 336 KPYECSECGKAFRQSIHLTQHLRIHTGEKPYQCG--ECGKAFSHSSSLTKHQRIHTGEKPYE------------------ 395
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLnskslplsnskassssls 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 396 -----------CHECGKAFTQITPLIQ--HQRTHTGEKPYE-CSECGKAFSQSTLL-------------------TEHRR 442
Cdd:COG5048   112 ssssnsndnnlLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 443 IHTGEKPYGCNECGKTFSHSSSLSQHERTHTGEKPYECSQCGKAFRQS------THLTQHQRIHTGEKPYECNDCGKAFS 516
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsqspSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 517 HSSSLTKHQRIHTG-EKPYECNQCGRAFSQLAPLIQHQR--IHTGE--KPYEC--NQCGRAFSQSSLLIEHQRIHTKEKP 589
Cdd:COG5048   272 SSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 590 YGCNEC-------GKSFSHSSSLSQHERTHTGEKPYEC--HDCGKSFRQSTHLTQHRRIHTGEKPYVCRD--CGKAFTHS 658
Cdd:COG5048   352 AKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRH 431

                         410
                  ....*....|.
gi 1622893442 659 SSLTKHQRTHT 669
Cdd:COG5048   432 YNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
265-436 3.40e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 265 NSSALTKHQRIHTgekPYKCTQCGRTFNQIAPLIQHQRT--HTGE--KPYECSE--CGKSFSFRSSFSQHERTHTGEKPY 338
Cdd:COG5048   276 NESDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 339 EC--SECGKAFRQSIH--LTQHLRIHTGEKPYQCGE-----CGKAFSHSSSLTKHQRIHTGEKPYECH--ECGKAFTQIT 407
Cdd:COG5048   353 KEklLNSSSKFSPLLNnePPQSLQQYKDLKNDKKSEtlsnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHY 432

                         170       180
                  ....*....|....*....|....*....
gi 1622893442 408 PLIQHQRTHTGEKPYECSECGKAFSQSTL 436
Cdd:COG5048   433 NLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-405 1.32e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.32e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 380 SLTKHQRIHTGEKPYECHECGKAFTQ 405
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
492-517 1.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.34e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 492 HLTQHQRIHTGEKPYECNDCGKAFSH 517
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
464-489 1.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.46e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 464 SLSQHERTHTGEKPYECSQCGKAFRQ 489
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
352-377 1.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.53e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 352 HLTQHLRIHTGEKPYQCGECGKAFSH 377
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
409-433 2.00e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.00e-04
                          10        20
                  ....*....|....*....|....*
gi 1622893442 409 LIQHQRTHTGEKPYECSECGKAFSQ 433
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
632-657 3.82e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.82e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 632 HLTQHRRIHTGEKPYVCRDCGKAFTH 657
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
268-293 3.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.93e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 268 ALTKHQRIHTGEKPYKCTQCGRTFNQ 293
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
327-349 5.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.33e-04
                          10        20
                  ....*....|....*....|...
gi 1622893442 327 QHERTHTGEKPYECSECGKAFRQ 349
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
520-545 5.82e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.82e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 520 SLTKHQRIHTGEKPYECNQCGRAFSQ 545
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
607-629 6.42e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.42e-04
                          10        20
                  ....*....|....*....|...
gi 1622893442 607 QHERTHTGEKPYECHDCGKSFRQ 629
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 506-528 7.64e-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: 7.64e-04
                          10        20
                  ....*....|....*....|...
gi 1622893442 506 YECNDCGKAFSHSSSLTKHQRIH 528
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
549-573 7.74e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.74e-04
                          10        20
                  ....*....|....*....|....*
gi 1622893442 549 LIQHQRIHTGEKPYECNQCGRAFSQ 573
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 618-640 1.11e-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: 36.51  E-value: 1.11e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 618 YECHDCGKSFRQSTHLTQHRRIH 640
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 646-668 1.19e-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: 36.51  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 646 YVCRDCGKAFTHSSSLTKHQRTH 668
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 334-417 1.31e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 334 GEKPYECS--ECGKAFRQSIHLTQHlRIHtgekpyqcGECGKAFSHSSSLTKHQRIHTGEKPYECHECGKAFTQITPLIQ 411
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1622893442 412 HqRTHT 417
Cdd:COG5189   417 H-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 366-388 1.46e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 366 YQCGECGKAFSHSSSLTKHQRIH 388
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 254-276 1.58e-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: 1.58e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 254 YECHECGKGFRNSSALTKHQRIH 276
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 221-305 3.14e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622893442 221 VKEKPYKCQ--ECRKAFSHSSALiEHHRTHtGERPYECHEcgkgfrnSSALTKHQRIHTGEKPYKCTQCGRTFNQIAPLI 298
Cdd:COG5189   345 KDGKPYKCPveGCNKKYKNQNGL-KYHMLH-GHQNQKLHE-------NPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                  ....*..
gi 1622893442 299 QHqRTHT 305
Cdd:COG5189   416 YH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
240-265 3.95e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.95e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622893442 240 ALIEHHRTHTGERPYECHECGKGFRN 265
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 478-500 6.23e-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: 6.23e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 478 YECSQCGKAFRQSTHLTQHQRIH 500
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
297-317 6.65e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.65e-03
                          10        20
                  ....*....|....*....|.
gi 1622893442 297 LIQHQRTHTGEKPYECSECGK 317
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGK 22
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 532-588 7.36e-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: 7.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622893442 532 KPYeCNQCGRAFSQLAPLIQHQRIHTgekpYECNQCGRAFSQSSLLIEH-QRIHtKEK 588
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH-KET 52
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 338-360 8.88e-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: 8.88e-03
                          10        20
                  ....*....|....*....|...
gi 1622893442 338 YECSECGKAFRQSIHLTQHLRIH 360
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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