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Conserved domains on  [gi|116875834|ref|NP_003417|]
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zinc finger protein 74 isoform a [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204378)

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 smart00349
krueppel associated box;
43-103 2.38e-34

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 124.63  E-value: 2.38e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116875834    43 VSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLALGPPLHKPDVISHLERGEEPWS 103
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-511 1.62e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.11  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 331 PYKCSACEKAFSCSSLLSMHLR--VHTGE--KPYRCGE--CGKAFNQRTHLTRHHRIHTGEKPYQC--GSCGKAFT---- 398
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSplln 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 399 -CHSSLTVHEKIHSGDKPFKCSD--CEKAFNSRSRLTLHQRTHTGEKPfkcadcgkgfschayllvhrrihsgeKPFKCN 475
Cdd:COG5048  369 nEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRP--------------------------YNCKNP 422

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116875834 476 ECGKAFSSHAYLIVHRRIHTGEKPFDCSQCWKAFSC 511
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-395 6.22e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 248 FVCGECGKAFRQSSSLTLHRRW--HSRE--KAYKCDE--CGKAFTWSTNLLEHRRIHTGEKPFFC--GECGKAFS----- 314
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnn 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 315 CHSSLNVHQRIHTGERPYKC--SACEKAFSCSSLLSMHLRVHTGEKP--YRCGECGKAFNQRTHLTRHHRIHTGEKPYQC 390
Cdd:COG5048  370 EPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449


                 ....*
gi 116875834 391 GSCGK 395
Cdd:COG5048  450 SILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
514-539 1.25e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  514 SLIVHQRIHTGEKPYKCSECGRAFSQ 539
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
43-103 2.38e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 124.63  E-value: 2.38e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116875834    43 VSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLALGPPLHKPDVISHLERGEEPWS 103
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 42-83 2.26e-23

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: 92.92  E-value: 2.26e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116875834   42 SVSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLALG 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 43-82 1.94e-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: 81.83  E-value: 1.94e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 116875834  43 VSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLAL 82
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-511 1.62e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.11  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 331 PYKCSACEKAFSCSSLLSMHLR--VHTGE--KPYRCGE--CGKAFNQRTHLTRHHRIHTGEKPYQC--GSCGKAFT---- 398
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSplln 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 399 -CHSSLTVHEKIHSGDKPFKCSD--CEKAFNSRSRLTLHQRTHTGEKPfkcadcgkgfschayllvhrrihsgeKPFKCN 475
Cdd:COG5048  369 nEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRP--------------------------YNCKNP 422

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116875834 476 ECGKAFSSHAYLIVHRRIHTGEKPFDCSQCWKAFSC 511
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
zf-H2C2_2 pfam13465
Zinc-finger double domain;
374-399 4.46e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.46e-05
                          10        20
                  ....*....|....*....|....*.
gi 116875834  374 HLTRHHRIHTGEKPYQCGSCGKAFTC 399
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-395 6.22e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 248 FVCGECGKAFRQSSSLTLHRRW--HSRE--KAYKCDE--CGKAFTWSTNLLEHRRIHTGEKPFFC--GECGKAFS----- 314
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnn 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 315 CHSSLNVHQRIHTGERPYKC--SACEKAFSCSSLLSMHLRVHTGEKP--YRCGECGKAFNQRTHLTRHHRIHTGEKPYQC 390
Cdd:COG5048  370 EPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449


                 ....*
gi 116875834 391 GSCGK 395
Cdd:COG5048  450 SILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
514-539 1.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  514 SLIVHQRIHTGEKPYKCSECGRAFSQ 539
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
318-343 1.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  318 SLNVHQRIHTGERPYKCSACEKAFSC 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 498-546 9.76e-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: 35.61  E-value: 9.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116875834 498 KPFdCSQCWKAFSCHSSLIVHQRIHTgekpYKCSECGRAFS-----QNHCLIKH 546
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYtagglAVHCLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
43-103 2.38e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 124.63  E-value: 2.38e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116875834    43 VSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLALGPPLHKPDVISHLERGEEPWS 103
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 42-83 2.26e-23

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: 92.92  E-value: 2.26e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116875834   42 SVSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLALG 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 43-82 1.94e-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: 81.83  E-value: 1.94e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 116875834  43 VSFKDVAVDFTQEEWGQLDSPQRALYRDVMLENYQNLLAL 82
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-511 1.62e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.11  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 331 PYKCSACEKAFSCSSLLSMHLR--VHTGE--KPYRCGE--CGKAFNQRTHLTRHHRIHTGEKPYQC--GSCGKAFT---- 398
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSplln 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 399 -CHSSLTVHEKIHSGDKPFKCSD--CEKAFNSRSRLTLHQRTHTGEKPfkcadcgkgfschayllvhrrihsgeKPFKCN 475
Cdd:COG5048  369 nEPPQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRP--------------------------YNCKNP 422

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116875834 476 ECGKAFSSHAYLIVHRRIHTGEKPFDCSQCWKAFSC 511
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
317-542 4.55e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 4.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 317 SSLNVHQRIHTGERPYKCSACEKAFSCSSLLSMHLRVHTGEKPYRCGECGKAFNQRTHLTRHHRIHTGE-------KPYQ 389
Cdd:COG5048  212 PSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIK 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 390 CGSCGKAFTCHSSLTVH--EKIHSG--DKPFKC--SDCEKAFNSRSRLTLHQRTHTGEKPFKC--ADCGKGFS-----CH 456
Cdd:COG5048  292 SKQCNISFSRSSPLTRHlrSVNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEP 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 457 AYLLVHRRIHSGEKPFKC--NECGKAFSSHAYLIVHRRIHTGEKP--FDCSQCWKAFSCHSSLIVHQRIHTGEKPYKCSE 532
Cdd:COG5048  372 PQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSI 451

                        250
                 ....*....|
gi 116875834 533 CGRAFSQNHC 542
Cdd:COG5048  452 LKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
276-558 7.96e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.17  E-value: 7.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 276 YKCDECGKAFTWSTNLLEHRRIHTGEKPFFCGECGKAFSCHSSLN--VHQRIHTGERPYKCSAC-----EKAFSCS-SLL 347
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLElsRHLRTHHNNPSDLNSKSlplsnSKASSSSlSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 348 SMHLRVHTGEKPyrCGECGKAFNQRTHLTRHHRIHTGEKPYQCGSCGKAF-------------------TCHSSLTVHEK 408
Cdd:COG5048  114 SSNSNDNNLLSS--HSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqsnslhpplpanslskdpSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 409 IHSGDKPFKCSDCEKAFNSRSRLTLHQRTHTGEKPFKCADCGKGFSCHAYLLVHRRIHSGEKPFKCNECGKAFSSHAYLI 488
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 489 VHRRIHTGE-------KPFDCSQCWKAFSCHSSLIVHQR--IHTGE--KPYKCSE--CGRAFSQNHCLIKHQKIHSGEKS 555
Cdd:COG5048  272 SSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351


                 ...
gi 116875834 556 FKC 558
Cdd:COG5048  352 AKE 354
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
247-584 1.50e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 247 EFVCGECGKAFRQSSSLTLHRRWHSREKAYKC--DECGKAFTWSTNLLEHRRIHTGEKPFFC----------------GE 308
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSS 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 309 CGKAFS-------------------------CHSSLNVHQRIHTGERPYKCSA-----------CEKAFSCSSLLSmHLR 352
Cdd:COG5048  113 SSSNSNdnnllsshslppssrdpqlpdllsiSNLRNNPLPGNNSSSVNTPQSNslhpplpanslSKDPSSNLSLLI-SSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 353 VHTGEKPYRCGECGKAFNQRTHLTRHHRIHTGEKPYQCGSCGKAFTCH------SSLTVHEKIHSGDKPFKCSDCEKAFN 426
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSllsqspSSLSSSDSSSSASESPRSSLPTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 427 SRSRLTLHQRTHTG-EKPFKCADCGKGFSCHAYLLVHRR--IHSGE--KPFKCNE--CGKAFSSHAYLIVHRRIHTGEKP 499
Cdd:COG5048  272 SSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 500 FDC--SQCWKAFS-----CHSSLIVHQRIHTGEKPYKC--SECGRAFSQNHCLIKH--QKIHSGEKSFKCEKCGEMFNWS 568
Cdd:COG5048  352 AKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRH 431

                        410
                 ....*....|....*.
gi 116875834 569 SHLTEHQRLHSEGKPL 584
Cdd:COG5048  432 YNLIPHKKIHTNHAPL 447
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
302-579 3.00e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 302 KPFFCGECGKAFSCHSSLNVHQRIHTGERPYKCSACEKAFSCSSLLSM--HLRVHTGEKPYRC-GECGKAFNQRTHLTRH 378
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 379 HRIHTGEKPYQCGSCGKAFTCHSSLTVHEKIHS-------GDKPFKCSDCEKAFNSRSRLTLHqRTHTGEKPFKCADCGK 451
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrnnplPGNNSSSVNTPQSNSLHPPLPAN-SLSKDPSSNLSLLISS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 452 GFSCHAY------LLVHRRI--HSGEKPFKCNECGKAFSSHAYLIVH----RRIHTGEKPFDCSQCWKAFSCHSSLIVHQ 519
Cdd:COG5048  191 NVSTSIPsssensPLSSSYSipSSSSDQNLENSSSSLPLTTNSQLSPksllSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116875834 520 RIHTG-----------EKPYKCSECGRAFSQNHCLIKHQ--KIHSGE--KSFKC--EKCGEMFNWSSHLTEHQRLHS 579
Cdd:COG5048  271 QSSSPnesdsssekgfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347
zf-H2C2_2 pfam13465
Zinc-finger double domain;
374-399 4.46e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.46e-05
                          10        20
                  ....*....|....*....|....*.
gi 116875834  374 HLTRHHRIHTGEKPYQCGSCGKAFTC 399
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-395 6.22e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 248 FVCGECGKAFRQSSSLTLHRRW--HSRE--KAYKCDE--CGKAFTWSTNLLEHRRIHTGEKPFFC--GECGKAFS----- 314
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnn 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875834 315 CHSSLNVHQRIHTGERPYKC--SACEKAFSCSSLLSMHLRVHTGEKP--YRCGECGKAFNQRTHLTRHHRIHTGEKPYQC 390
Cdd:COG5048  370 EPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449


                 ....*
gi 116875834 391 GSCGK 395
Cdd:COG5048  450 SILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
347-371 1.22e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|....*
gi 116875834  347 LSMHLRVHTGEKPYRCGECGKAFNQ 371
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
514-539 1.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  514 SLIVHQRIHTGEKPYKCSECGRAFSQ 539
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
318-343 1.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  318 SLNVHQRIHTGERPYKCSACEKAFSC 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-483 1.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.40e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  458 YLLVHRRIHSGEKPFKCNECGKAFSS 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-315 2.96e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.96e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  290 NLLEHRRIHTGEKPFFCGECGKAFSC 315
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-455 3.60e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.60e-04
                          10        20
                  ....*....|....*....|....*.
gi 116875834  430 RLTLHQRTHTGEKPFKCADCGKGFSC 455
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 360-382 9.30e-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: 36.89  E-value: 9.30e-04
                          10        20
                  ....*....|....*....|...
gi 116875834  360 YRCGECGKAFNQRTHLTRHHRIH 382
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 528-550 2.38e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.38e-03
                          10        20
                  ....*....|....*....|...
gi 116875834  528 YKCSECGRAFSQNHCLIKHQKIH 550
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
413-475 2.45e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 2.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116875834 413 DKPFKCSDCEKAFNSRSRLTLHQRTHTGEKPFKCADCGKGFSCHAY--LLVHRRIHSGEKPFKCN 475
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNS 95
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 472-494 3.17e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.17e-03
                          10        20
                  ....*....|....*....|...
gi 116875834  472 FKCNECGKAFSSHAYLIVHRRIH 494
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 248-270 6.06e-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: 6.06e-03
                          10        20
                  ....*....|....*....|...
gi 116875834  248 FVCGECGKAFRQSSSLTLHRRWH 270
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 416-438 8.05e-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: 34.20  E-value: 8.05e-03
                          10        20
                  ....*....|....*....|...
gi 116875834  416 FKCSDCEKAFNSRSRLTLHQRTH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 498-546 9.76e-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: 35.61  E-value: 9.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116875834 498 KPFdCSQCWKAFSCHSSLIVHQRIHTgekpYKCSECGRAFS-----QNHCLIKH 546
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYtagglAVHCLQVH 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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