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Conserved domains on  [gi|289547701|ref|NP_115973|]
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zinc finger protein 347 isoform b [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-66 8.77e-29

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.22  E-value: 8.77e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 289547701     8 VTFRDVAIEFSQEEWTCLDPAQRTLYRDVMLENYRNLASLGISCFDLSIISMLEQGKEP 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-727 1.39e-17

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 86.67  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 272 QNSHLASHQRSHT------KEKPYKCYECGKAFRTRSNLTTHQVIHTGEKRYKCN--ECGKVFSRNSQLSQHQKIHTGEK 343
Cdd:COG5048   11 SNNSVLSSTPKSTlkslsnAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 344 PYKCN-ECGKVFTQNSHLVRHRGIHTGEKPYKCNECGKAFRARSSLAI--HQATHSGEKPYK-CNECGKVFTQ-NSHLTN 418
Cdd:COG5048   91 SDLNSkSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQsNSLHPP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 419 HWRIHTGEKPYKCNecgkafgvrsSLAIHLVIHTGEKPYKCHECGKVFRRNSHLARHQLIHTGEKPYKCNECGKAFRAHS 498
Cdd:COG5048  171 LPANSLSKDPSSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 499 NLTTHQVIHTGEKPYKCNECGKVFTQNSHLANHQRIHTGV-------KPYMCNECGKAFSVYSSLTTHQ--VIHTGE--K 567
Cdd:COG5048  241 LSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 568 PYKCNE--CGKVFTQNSHLARHRGIHTGEKPYKC--NECGKVFRHNSYLSRHQRIHtgekPYKYNEYGKAFSEHSnltth 643
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ----QYKDLKNDKKSETLS----- 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 644 qvihtgekpykcNECGKVFTQNSHLARHRRVHTGGKPYQCN--ECGKAFSQTSKLARHQRVHTGEKPYECNQCGKaFSVR 721
Cdd:COG5048  392 ------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRD 458


                 ....*.
gi 289547701 722 SSLTTH 727
Cdd:COG5048  459 LDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
722-816 1.61e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 722 SSLTTHQAIHTGKKPYKCNECGKVFTQNSHLARHRGIHTGEKPYKCN--ECGKAFSQTSKLARHQRIHTGEKPYECGKPF 799
Cdd:COG5048   19 TPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSL 98

                         90
                 ....*....|....*..
gi 289547701 800 SICSSLTTHQTIHTGGK 816
Cdd:COG5048   99 PLSNSKASSSSLSSSSS 115
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-66 8.77e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.22  E-value: 8.77e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 289547701     8 VTFRDVAIEFSQEEWTCLDPAQRTLYRDVMLENYRNLASLGISCFDLSIISMLEQGKEP 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 8-48 1.68e-25

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: 99.08  E-value: 1.68e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 289547701    8 VTFRDVAIEFSQEEWTCLDPAQRTLYRDVMLENYRNLASLG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-47 2.38e-21

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: 87.22  E-value: 2.38e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 289547701   8 VTFRDVAIEFSQEEWTCLDPAQRTLYRDVMLENYRNLASL 47
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-727 1.39e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 86.67  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 272 QNSHLASHQRSHT------KEKPYKCYECGKAFRTRSNLTTHQVIHTGEKRYKCN--ECGKVFSRNSQLSQHQKIHTGEK 343
Cdd:COG5048   11 SNNSVLSSTPKSTlkslsnAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 344 PYKCN-ECGKVFTQNSHLVRHRGIHTGEKPYKCNECGKAFRARSSLAI--HQATHSGEKPYK-CNECGKVFTQ-NSHLTN 418
Cdd:COG5048   91 SDLNSkSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQsNSLHPP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 419 HWRIHTGEKPYKCNecgkafgvrsSLAIHLVIHTGEKPYKCHECGKVFRRNSHLARHQLIHTGEKPYKCNECGKAFRAHS 498
Cdd:COG5048  171 LPANSLSKDPSSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 499 NLTTHQVIHTGEKPYKCNECGKVFTQNSHLANHQRIHTGV-------KPYMCNECGKAFSVYSSLTTHQ--VIHTGE--K 567
Cdd:COG5048  241 LSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 568 PYKCNE--CGKVFTQNSHLARHRGIHTGEKPYKC--NECGKVFRHNSYLSRHQRIHtgekPYKYNEYGKAFSEHSnltth 643
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ----QYKDLKNDKKSETLS----- 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 644 qvihtgekpykcNECGKVFTQNSHLARHRRVHTGGKPYQCN--ECGKAFSQTSKLARHQRVHTGEKPYECNQCGKaFSVR 721
Cdd:COG5048  392 ------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRD 458


                 ....*.
gi 289547701 722 SSLTTH 727
Cdd:COG5048  459 LDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
722-816 1.61e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 722 SSLTTHQAIHTGKKPYKCNECGKVFTQNSHLARHRGIHTGEKPYKCN--ECGKAFSQTSKLARHQRIHTGEKPYECGKPF 799
Cdd:COG5048   19 TPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSL 98

                         90
                 ....*....|....*..
gi 289547701 800 SICSSLTTHQTIHTGGK 816
Cdd:COG5048   99 PLSNSKASSSSLSSSSS 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-300 2.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|....*.
gi 289547701  275 HLASHQRSHTKEKPYKCYECGKAFRT 300
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
751-776 2.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.94e-04
                          10        20
                  ....*....|....*....|....*.
gi 289547701  751 HLARHRGIHTGEKPYKCNECGKAFSQ 776
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 318-363 9.98e-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: 9.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 289547701 318 KCNECGKVFSRNSQLSQHQKIHTgekpYKCNECGKVFTQNSHLVRH 363
Cdd:cd20908    3 WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-66 8.77e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 109.22  E-value: 8.77e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 289547701     8 VTFRDVAIEFSQEEWTCLDPAQRTLYRDVMLENYRNLASLGISCFDLSIISMLEQGKEP 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEP 59
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 8-48 1.68e-25

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: 99.08  E-value: 1.68e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 289547701    8 VTFRDVAIEFSQEEWTCLDPAQRTLYRDVMLENYRNLASLG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-47 2.38e-21

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: 87.22  E-value: 2.38e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 289547701   8 VTFRDVAIEFSQEEWTCLDPAQRTLYRDVMLENYRNLASL 47
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-727 1.39e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 86.67  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 272 QNSHLASHQRSHT------KEKPYKCYECGKAFRTRSNLTTHQVIHTGEKRYKCN--ECGKVFSRNSQLSQHQKIHTGEK 343
Cdd:COG5048   11 SNNSVLSSTPKSTlkslsnAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 344 PYKCN-ECGKVFTQNSHLVRHRGIHTGEKPYKCNECGKAFRARSSLAI--HQATHSGEKPYK-CNECGKVFTQ-NSHLTN 418
Cdd:COG5048   91 SDLNSkSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQsNSLHPP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 419 HWRIHTGEKPYKCNecgkafgvrsSLAIHLVIHTGEKPYKCHECGKVFRRNSHLARHQLIHTGEKPYKCNECGKAFRAHS 498
Cdd:COG5048  171 LPANSLSKDPSSNL----------SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 499 NLTTHQVIHTGEKPYKCNECGKVFTQNSHLANHQRIHTGV-------KPYMCNECGKAFSVYSSLTTHQ--VIHTGE--K 567
Cdd:COG5048  241 LSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 568 PYKCNE--CGKVFTQNSHLARHRGIHTGEKPYKC--NECGKVFRHNSYLSRHQRIHtgekPYKYNEYGKAFSEHSnltth 643
Cdd:COG5048  321 PFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ----QYKDLKNDKKSETLS----- 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 644 qvihtgekpykcNECGKVFTQNSHLARHRRVHTGGKPYQCN--ECGKAFSQTSKLARHQRVHTGEKPYECNQCGKaFSVR 721
Cdd:COG5048  392 ------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRD 458


                 ....*.
gi 289547701 722 SSLTTH 727
Cdd:COG5048  459 LDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
455-810 1.02e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 74.35  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 455 KPYKCHECGKVFRRNSHLARHQLIHTGEKPYKCN--ECGKAFRAHSNLTTHQVIHTGEKPYKCN-ECGKVFTQNSHLANH 531
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 532 QRIHTGVKPYMCNECGKAFSVYSSLT--THQVIHTGEKPYK-CNECGKVFTQ-NSHLARHRGIHTGEKPYKCNECGKVFR 607
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLpdLLSISNLRNNPLPgNNSSSVNTPQsNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 608 HNSYLSRHQRIHTGEKPYKY-NEYGKAFSEHSN--LTTHQVIHTGEKPYK---------------CNECGKVFTQNSHLA 669
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIpSSSSDQNLENSSssLPLTTNSQLSPKSLLsqspsslsssdssssASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 670 RHRRVHTG-------GKPYQCNECGKAFSQTSKLARHQR--VHTGE--KPYEC--NQCGKAFSVRSSLTTHQAIHTGKKP 736
Cdd:COG5048  272 SSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 737 YKC--NECGKVFTQNSH-----LARHRGIHTGEKPYKC--NECGKAFSQTSKLARHQRIHTGEKPYECgkPFSICSSLTT 807
Cdd:COG5048  352 AKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNC--KNPPCSKSFN 429


                 ...
gi 289547701 808 HQT 810
Cdd:COG5048  430 RHY 432
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
511-820 7.01e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 7.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 511 KPYKCNECGKVFTQNSHLANHQRIHTGVKPYMCN--ECGKAFSVYSSLTTHQVIHTGEKPYKCN-ECGKVFTQNSHLARH 587
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 588 RGIHTGEKPYKCNECGKVFRHNSYL--SRHQRIHTGEKPYKYNEYGKAFSEHSNLTTHQVIHtgekpykcNECGKVFTQN 665
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQlpDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPA--------NSLSKDPSSN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 666 SHLARHRRVHTGGKPYQCNECGKAFSQTSKLARHQRVHTGEKPYECNQCGKAF--SVRSSLTTHQAIHTGKKPykCNECG 743
Cdd:COG5048  184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpkSLLSQSPSSLSSSDSSSS--ASESP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 744 KVFTQNSHLARHRGIHTGE-------KPYKCNECGKAFSQTSKLARHQR--IHTGE--KPYEC-----GKPFSICSSLTT 807
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpyslcGKLFSRNDALKR 341

                        330
                 ....*....|...
gi 289547701 808 HQTIHTGGKPYKC 820
Cdd:COG5048  342 HILLHTSISPAKE 354
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
260-616 1.85e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.95  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 260 PYKSNGCGMVFPQNSHLASHQRSHTKEKPYKCY--ECGKAFRTRSNLTTHQVIHTGEKRYKC----------------NE 321
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSS 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 322 CGKVFSRNSQLSQH---------------QKIHTGEKPYK-CNECGKVFTQ-NSHLVRHRGIHTGEKPYK---------- 374
Cdd:COG5048  113 SSSNSNDNNLLSSHslppssrdpqlpdllSISNLRNNPLPgNNSSSVNTPQsNSLHPPLPANSLSKDPSSnlsllissnv 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 375 --------CNECGKAFRARSSLAIHQATHSGEKPYKCNECGKVFT------QNSHLTNHWRIHTGEKPYKCNECGKAFGV 440
Cdd:COG5048  193 stsipsssENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPksllsqSPSSLSSSDSSSSASESPRSSLPTASSQS 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 441 RSSLAIHLVIHTG-EKPYKCHECGKVFRRNSHLARHQ--LIHTGE--KPYKCNE--CGKAFRAHSNLTTHQVIHTGEKPY 513
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 514 KC--NECGKVFTQNSHLANHQRIH-----TGVKPYMC--NECGKAFSVYSSLTTHQVIHTGEKPY--KCNECGKVFTQNS 582
Cdd:COG5048  353 KEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHY 432

                        410       420       430
                 ....*....|....*....|....*....|....
gi 289547701 583 HLARHRGIHTGEKPYKCNECGKVFRHNSYLSRHQ 616
Cdd:COG5048  433 NLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
722-816 1.61e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 722 SSLTTHQAIHTGKKPYKCNECGKVFTQNSHLARHRGIHTGEKPYKCN--ECGKAFSQTSKLARHQRIHTGEKPYECGKPF 799
Cdd:COG5048   19 TPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSL 98

                         90
                 ....*....|....*..
gi 289547701 800 SICSSLTTHQTIHTGGK 816
Cdd:COG5048   99 PLSNSKASSSSLSSSSS 115
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-300 2.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|....*.
gi 289547701  275 HLASHQRSHTKEKPYKCYECGKAFRT 300
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
471-494 2.83e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.83e-04
                          10        20
                  ....*....|....*....|....
gi 289547701  471 HLARHQLIHTGEKPYKCNECGKAF 494
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
751-776 2.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.94e-04
                          10        20
                  ....*....|....*....|....*.
gi 289547701  751 HLARHRGIHTGEKPYKCNECGKAFSQ 776
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
332-356 3.09e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.09e-04
                          10        20
                  ....*....|....*....|....*
gi 289547701  332 LSQHQKIHTGEKPYKCNECGKVFTQ 356
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
696-719 3.38e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.38e-04
                          10        20
                  ....*....|....*....|....
gi 289547701  696 LARHQRVHTGEKPYECNQCGKAFS 719
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
667-692 5.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 289547701  667 HLARHRRVHTGGKPYQCNECGKAFSQ 692
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 457-479 6.31e-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: 37.66  E-value: 6.31e-04
                          10        20
                  ....*....|....*....|...
gi 289547701  457 YKCHECGKVFRRNSHLARHQLIH 479
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 653-675 7.38e-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: 7.38e-04
                          10        20
                  ....*....|....*....|...
gi 289547701  653 YKCNECGKVFTQNSHLARHRRVH 675
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
583-608 9.37e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 9.37e-04
                          10        20
                  ....*....|....*....|....*.
gi 289547701  583 HLARHRGIHTGEKPYKCNECGKVFRH 608
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-382 9.47e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 9.47e-04
                          10        20
                  ....*....|....*....|....
gi 289547701  359 HLVRHRGIHTGEKPYKCNECGKAF 382
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 513-535 1.03e-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: 36.89  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  513 YKCNECGKVFTQNSHLANHQRIH 535
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 597-619 1.12e-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: 36.89  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  597 YKCNECGKVFRHNSYLSRHQRIH 619
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
499-524 1.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547701  499 NLTTHQVIHTGEKPYKCNECGKVFTQ 524
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
639-664 1.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547701  639 NLTTHQVIHTGEKPYKCNECGKVFTQ 664
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 401-423 1.50e-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: 1.50e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  401 YKCNECGKVFTQNSHLTNHWRIH 423
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
723-748 1.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547701  723 SLTTHQAIHTGKKPYKCNECGKVFTQ 748
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
527-551 2.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.34e-03
                          10        20
                  ....*....|....*....|....*
gi 289547701  527 HLANHQRIHTGVKPYMCNECGKAFS 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 317-339 2.44e-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: 2.44e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  317 YKCNECGKVFSRNSQLSQHQKIH 339
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-580 2.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.96e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547701  555 SLTTHQVIHTGEKPYKCNECGKVFTQ 580
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 509-589 3.45e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 509 GEKPYKCN--ECGKVFTQNSHLANHqRIHtgvkpymcNECGKAFSVYSSLTTHQVIHTGEKPYKCNECGKVFTQNSHLAR 586
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ...
gi 289547701 587 HRG 589
Cdd:COG5189  417 HRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
387-412 3.60e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.60e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547701  387 SLAIHQATHSGEKPYKCNECGKVFTQ 412
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
415-438 4.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 4.51e-03
                          10        20
                  ....*....|....*....|....
gi 289547701  415 HLTNHWRIHTGEKPYKCNECGKAF 438
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 286-365 4.51e-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: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 286 EKPYKC--YECGKAFRTRSNLTTHQvihtgekryKCNECGKVFSRNSQLSQHQKIHTGEKPYKCNECGKVFTQNSHLVRH 363
Cdd:COG5189  347 GKPYKCpvEGCNKKYKNQNGLKYHM---------LHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417


                 ..
gi 289547701 364 RG 365
Cdd:COG5189  418 RK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
443-468 5.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.33e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547701  443 SLAIHLVIHTGEKPYKCHECGKVFRR 468
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-328 5.77e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.77e-03
                          10        20
                  ....*....|....*....|....*.
gi 289547701  303 NLTTHQVIHTGEKRYKCNECGKVFSR 328
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 765-787 5.97e-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: 5.97e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  765 YKCNECGKAFSQTSKLARHQRIH 787
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 681-703 7.05e-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: 7.05e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  681 YQCNECGKAFSQTSKLARHQRVH 703
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 569-591 7.19e-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: 34.58  E-value: 7.19e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  569 YKCNECGKVFTQNSHLARHRGIH 591
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 737-759 7.19e-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: 34.58  E-value: 7.19e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  737 YKCNECGKVFTQNSHLARHRGIH 759
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 672-757 7.38e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547701 672 RRVHTGGKPYQCN--ECGKAFSQTSKLARHqRVHtgekpyecNQCGKAFSVRSSLTTHQAIHTGKKPYKCNECGKVFTQN 749
Cdd:COG5189  341 MLKVKDGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNL 411


                 ....*...
gi 289547701 750 SHLARHRG 757
Cdd:COG5189  412 NGLKYHRK 419
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 345-367 8.01e-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: 34.58  E-value: 8.01e-03
                          10        20
                  ....*....|....*....|...
gi 289547701  345 YKCNECGKVFTQNSHLVRHRGIH 367
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 318-363 9.98e-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: 9.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 289547701 318 KCNECGKVFSRNSQLSQHQKIHTgekpYKCNECGKVFTQNSHLVRH 363
Cdd:cd20908    3 WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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