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Conserved domains on  [gi|154800449|ref|NP_003424|]
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zinc finger protein 132 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 37-78 1.52e-21

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: 87.91  E-value: 1.52e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154800449   37 MVTFEDVAVYFSQEEWELLDAAQRHLYHSVMLENLELVTSLG 78
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
105-528 1.43e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 105 NADPSTKKANSCDMCGPFLKDILHLAEHQGTQSEEKPYTCGACGRD--FWLNANLHQHQKEHSGGKPFRwYKDRDALMKS 182
Cdd:COG5048   25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDL-NSKSLPLSNS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 183 SKVHlSENPFTCREGGKVILGSCDLLQLQAVDSGQKPYSNLGQLPEVCTTQKLFECSNCGKAFLKSSTLPNHLRTHSEEI 262
Cdd:COG5048  104 KASS-SSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 263 PFTCPTGGNFLeeksilgnkkfhtgeIPHVCKECGKAFSHSSKLRKHQKFHTEVKYYECIACGK-TFNHKLTFVHHQR-- 339
Cdd:COG5048  183 NLSLLISSNVS---------------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTnSQLSPKSLLSQSPss 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 340 IHSGERPYECDECGKAFSNRSHLIRHEKVHTGER-------PFECLKCGRAFSQSSNFLRHQ--KVHTQ--VRPYEC--S 406
Cdd:COG5048  248 LSSSDSSSSASESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpyS 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 407 QCGKSFSRSSALIQHWRVHTGERPYECSECGRAFNNNSNL-------AQHQKVHTGERPFEC--SECGRDFSQSSHLLRH 477
Cdd:COG5048  328 LCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154800449 478 QKVHTGERP--FECCDCGKAFSNSSTLIQHQKVHTGQRPYECSECRKSFSRSS 528
Cdd:COG5048  408 IITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
383-706 3.10e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 383 AFSQSSNFLrHQKVHTQVRPYECSQCGKSFSRSSALIQHWRVHTGERPYECSECGRA--FNNNSNLAQHQKVHTGERPFE 460
Cdd:COG5048   15 VLSSTPKST-LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 461 CSEcgrDFSQSSHLLRHQKvhtgerPFECCDCGKAFSNSSTLIQHQKVHTGQRPYECSEC--------------RKSFSR 526
Cdd:COG5048   94 NSK---SLPLSNSKASSSS------LSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrnnplpgnnsssVNTPQS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 527 SSSLIQHWRIHTGEKPYECsecgkafahsSTLIEHWRVHTKERPYECNECGKFFSQNSILIKHQKVHTGEKPYKCSECGK 606
Cdd:COG5048  165 NSLHPPLPANSLSKDPSSN----------LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 607 FFSRksSLICHWRVHTGER--PYECSECGRAFSSNSHLVRHQRVHT-------QERPYECIQCGKAFSERSTLVRHQ--K 675
Cdd:COG5048  235 LSPK--SLLSQSPSSLSSSdsSSSASESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLrsV 312

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 154800449 676 VHTRE--RTYEC--SQCGKLFSHLCNLAQHKKIHT 706
Cdd:COG5048  313 NHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 37-78 1.52e-21

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: 87.91  E-value: 1.52e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154800449   37 MVTFEDVAVYFSQEEWELLDAAQRHLYHSVMLENLELVTSLG 78
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
38-78 3.91e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 3.91e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 154800449    38 VTFEDVAVYFSQEEWELLDAAQRHLYHSVMLENLELVTSLG 78
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 38-77 4.55e-19

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: 80.67  E-value: 4.55e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 154800449  38 VTFEDVAVYFSQEEWELLDAAQRHLYHSVMLENLELVTSL 77
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
105-528 1.43e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 105 NADPSTKKANSCDMCGPFLKDILHLAEHQGTQSEEKPYTCGACGRD--FWLNANLHQHQKEHSGGKPFRwYKDRDALMKS 182
Cdd:COG5048   25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDL-NSKSLPLSNS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 183 SKVHlSENPFTCREGGKVILGSCDLLQLQAVDSGQKPYSNLGQLPEVCTTQKLFECSNCGKAFLKSSTLPNHLRTHSEEI 262
Cdd:COG5048  104 KASS-SSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 263 PFTCPTGGNFLeeksilgnkkfhtgeIPHVCKECGKAFSHSSKLRKHQKFHTEVKYYECIACGK-TFNHKLTFVHHQR-- 339
Cdd:COG5048  183 NLSLLISSNVS---------------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTnSQLSPKSLLSQSPss 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 340 IHSGERPYECDECGKAFSNRSHLIRHEKVHTGER-------PFECLKCGRAFSQSSNFLRHQ--KVHTQ--VRPYEC--S 406
Cdd:COG5048  248 LSSSDSSSSASESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpyS 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 407 QCGKSFSRSSALIQHWRVHTGERPYECSECGRAFNNNSNL-------AQHQKVHTGERPFEC--SECGRDFSQSSHLLRH 477
Cdd:COG5048  328 LCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154800449 478 QKVHTGERP--FECCDCGKAFSNSSTLIQHQKVHTGQRPYECSECRKSFSRSS 528
Cdd:COG5048  408 IITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
383-706 3.10e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 383 AFSQSSNFLrHQKVHTQVRPYECSQCGKSFSRSSALIQHWRVHTGERPYECSECGRA--FNNNSNLAQHQKVHTGERPFE 460
Cdd:COG5048   15 VLSSTPKST-LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 461 CSEcgrDFSQSSHLLRHQKvhtgerPFECCDCGKAFSNSSTLIQHQKVHTGQRPYECSEC--------------RKSFSR 526
Cdd:COG5048   94 NSK---SLPLSNSKASSSS------LSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrnnplpgnnsssVNTPQS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 527 SSSLIQHWRIHTGEKPYECsecgkafahsSTLIEHWRVHTKERPYECNECGKFFSQNSILIKHQKVHTGEKPYKCSECGK 606
Cdd:COG5048  165 NSLHPPLPANSLSKDPSSN----------LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 607 FFSRksSLICHWRVHTGER--PYECSECGRAFSSNSHLVRHQRVHT-------QERPYECIQCGKAFSERSTLVRHQ--K 675
Cdd:COG5048  235 LSPK--SLLSQSPSSLSSSdsSSSASESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLrsV 312

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 154800449 676 VHTRE--RTYEC--SQCGKLFSHLCNLAQHKKIHT 706
Cdd:COG5048  313 NHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347
zf-H2C2_2 pfam13465
Zinc-finger double domain;
641-665 6.89e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.89e-04
                          10        20
                  ....*....|....*....|....*
gi 154800449  641 HLVRHQRVHTQERPYECIQCGKAFS 665
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-470 2.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|....*.
gi 154800449  445 NLAQHQKVHTGERPFECSECGRDFSQ 470
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 569-621 4.24e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.77  E-value: 4.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154800449 569 RPYeCNECGKFFSQNSILIKHQKvhtgEKPYKCSECGKFFSRKSSLICH-WRVH 621
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
PHA00733 PHA00733
hypothetical protein
 514-561 5.18e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 5.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 154800449 514 PYECSECRKSFSRSSSLIQHWRIHTGEKpyECSECGKAFAHSSTLIEH 561
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 485-537 5.21e-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: 36.38  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154800449 485 RPFeCCDCGKAFSNSSTLIQHQKVHTgqrpYECSECRKSFSRSSSLIQH-WRIH 537
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 37-78 1.52e-21

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: 87.91  E-value: 1.52e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154800449   37 MVTFEDVAVYFSQEEWELLDAAQRHLYHSVMLENLELVTSLG 78
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
38-78 3.91e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 3.91e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 154800449    38 VTFEDVAVYFSQEEWELLDAAQRHLYHSVMLENLELVTSLG 78
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 38-77 4.55e-19

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: 80.67  E-value: 4.55e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 154800449  38 VTFEDVAVYFSQEEWELLDAAQRHLYHSVMLENLELVTSL 77
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
105-528 1.43e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.41  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 105 NADPSTKKANSCDMCGPFLKDILHLAEHQGTQSEEKPYTCGACGRD--FWLNANLHQHQKEHSGGKPFRwYKDRDALMKS 182
Cdd:COG5048   25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDL-NSKSLPLSNS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 183 SKVHlSENPFTCREGGKVILGSCDLLQLQAVDSGQKPYSNLGQLPEVCTTQKLFECSNCGKAFLKSSTLPNHLRTHSEEI 262
Cdd:COG5048  104 KASS-SSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 263 PFTCPTGGNFLeeksilgnkkfhtgeIPHVCKECGKAFSHSSKLRKHQKFHTEVKYYECIACGK-TFNHKLTFVHHQR-- 339
Cdd:COG5048  183 NLSLLISSNVS---------------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTnSQLSPKSLLSQSPss 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 340 IHSGERPYECDECGKAFSNRSHLIRHEKVHTGER-------PFECLKCGRAFSQSSNFLRHQ--KVHTQ--VRPYEC--S 406
Cdd:COG5048  248 LSSSDSSSSASESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpyS 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 407 QCGKSFSRSSALIQHWRVHTGERPYECSECGRAFNNNSNL-------AQHQKVHTGERPFEC--SECGRDFSQSSHLLRH 477
Cdd:COG5048  328 LCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154800449 478 QKVHTGERP--FECCDCGKAFSNSSTLIQHQKVHTGQRPYECSECRKSFSRSS 528
Cdd:COG5048  408 IITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
345-677 8.35e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.72  E-value: 8.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 345 RPYECDECGKAFSNRSHLIRHEKVHTGERPFECLKCGRA--FSQSSNFLRHQKVHTQVRPYECSQCGKSFSRSSALIQhW 422
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSS-L 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 423 RVHTGERPYECSECGRAFNNNSNLAQHQKVHTGERPFEC--SECGRDFSQSSH--LLRHQKVHTgerpfecCDCGKAFSN 498
Cdd:COG5048  111 SSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNplPGNNSSSVNTPQsnSLHPPLPAN-------SLSKDPSSN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 499 SSTLIQHQKVHTGQRPYECSEcRKSFSRSSSLIQHWRIHTGEKPYECSECGKAFAHSSTLIEHWRVHTKERPYECNECGK 578
Cdd:COG5048  184 LSLLISSNVSTSIPSSSENSP-LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 579 FFSQNSILIKHQKVHTGE-------KPYKCSECGKFFSRKSSLICHWR--VHTGE--RPYECSE--CGRAFSSNSHLVRH 645
Cdd:COG5048  263 SSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                        330       340       350
                 ....*....|....*....|....*....|....
gi 154800449 646 QRVHTQERPYECI--QCGKAFSERSTLVRHQKVH 677
Cdd:COG5048  343 ILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
247-693 2.04e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 247 KSSTLPNHLRTHSEEIPFT--CP--TGGNFLEEKSILgNKKFHTGEIPHVC--KECGKAFSHSSKLRKHQKFHTEVKYYE 320
Cdd:COG5048   15 VLSSTPKSTLKSLSNAPRPdsCPncTDSFSRLEHLTR-HIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 321 CIACGKTFNHKLtfVHHQRIHSG-ERPYECDECGKAFSNRSHLIRHEKVHTGERPFECL--KCGRAF--SQSSNFLRHQK 395
Cdd:COG5048   94 NSKSLPLSNSKA--SSSSLSSSSsNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPlpGNNSSSvnTPQSNSLHPPL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 396 VHTqvrpyecSQCGKSFSRSSALIQHWRVHTGERPYECSECGRaFNNNSNLAQHQKVHTGERPFECSECGRDFSQSSHLL 475
Cdd:COG5048  172 PAN-------SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQ 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 476 RHQKVHTGERPFECCDCGKAFSNSSTLIQHQKVHTGQR-------PYECSECRKSFSRSSSLIQHWR--IHTGE--KPYE 544
Cdd:COG5048  244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 545 CSEcgkafahsstliehwrvhtkerpyecNECGKFFSQNSILIKHQKVHTGEKPYKCSEC-------GKFFSRKSSLICH 617
Cdd:COG5048  324 CPY--------------------------SLCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQ 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 618 WRVHTGERPYEC--SECGRAFSSNSHLVRHQRVHTQERPYEC--IQCGKAFSERSTLVRHQKVHTRERTYECSQCGKLFS 693
Cdd:COG5048  378 YKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
383-706 3.10e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 383 AFSQSSNFLrHQKVHTQVRPYECSQCGKSFSRSSALIQHWRVHTGERPYECSECGRA--FNNNSNLAQHQKVHTGERPFE 460
Cdd:COG5048   15 VLSSTPKST-LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 461 CSEcgrDFSQSSHLLRHQKvhtgerPFECCDCGKAFSNSSTLIQHQKVHTGQRPYECSEC--------------RKSFSR 526
Cdd:COG5048   94 NSK---SLPLSNSKASSSS------LSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrnnplpgnnsssVNTPQS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 527 SSSLIQHWRIHTGEKPYECsecgkafahsSTLIEHWRVHTKERPYECNECGKFFSQNSILIKHQKVHTGEKPYKCSECGK 606
Cdd:COG5048  165 NSLHPPLPANSLSKDPSSN----------LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800449 607 FFSRksSLICHWRVHTGER--PYECSECGRAFSSNSHLVRHQRVHT-------QERPYECIQCGKAFSERSTLVRHQ--K 675
Cdd:COG5048  235 LSPK--SLLSQSPSSLSSSdsSSSASESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLrsV 312

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 154800449 676 VHTRE--RTYEC--SQCGKLFSHLCNLAQHKKIHT 706
Cdd:COG5048  313 NHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347
zf-H2C2_2 pfam13465
Zinc-finger double domain;
641-665 6.89e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.89e-04
                          10        20
                  ....*....|....*....|....*
gi 154800449  641 HLVRHQRVHTQERPYECIQCGKAFS 665
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-470 2.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|....*.
gi 154800449  445 NLAQHQKVHTGERPFECSECGRDFSQ 470
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
586-610 2.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.33e-03
                          10        20
                  ....*....|....*....|....*
gi 154800449  586 LIKHQKVHTGEKPYKCSECGKFFSR 610
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
529-554 3.29e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.29e-03
                          10        20
                  ....*....|....*....|....*.
gi 154800449  529 SLIQHWRIHTGEKPYECSECGKAFAH 554
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
337-358 3.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.62e-03
                          10        20
                  ....*....|....*....|..
gi 154800449  337 HQRIHSGERPYECDECGKAFSN 358
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 627-649 4.18e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.18e-03
                          10        20
                  ....*....|....*....|...
gi 154800449  627 YECSECGRAFSSNSHLVRHQRVH 649
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 569-621 4.24e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.77  E-value: 4.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154800449 569 RPYeCNECGKFFSQNSILIKHQKvhtgEKPYKCSECGKFFSRKSSLICH-WRVH 621
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
361-386 4.73e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.73e-03
                          10        20
                  ....*....|....*....|....*.
gi 154800449  361 HLIRHEKVHTGERPFECLKCGRAFSQ 386
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
389-414 5.06e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.06e-03
                          10        20
                  ....*....|....*....|....*.
gi 154800449  389 NFLRHQKVHTQVRPYECSQCGKSFSR 414
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 514-561 5.18e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 5.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 154800449 514 PYECSECRKSFSRSSSLIQHWRIHTGEKpyECSECGKAFAHSSTLIEH 561
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 485-537 5.21e-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: 36.38  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154800449 485 RPFeCCDCGKAFSNSSTLIQHQKVHTgqrpYECSECRKSFSRSSSLIQH-WRIH 537
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 429-481 5.41e-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: 36.38  E-value: 5.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154800449 429 RPYeCSECGRAFNNNSNLAQHQKVHTgerpFECSECGRDFSQSSHLLRH-QKVH 481
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-H2C2_2 pfam13465
Zinc-finger double domain;
502-526 5.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.42e-03
                          10        20
                  ....*....|....*....|....*
gi 154800449  502 LIQHQKVHTGQRPYECSECRKSFSR 526
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 347-369 6.50e-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: 34.58  E-value: 6.50e-03
                          10        20
                  ....*....|....*....|...
gi 154800449  347 YECDECGKAFSNRSHLIRHEKVH 369
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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