NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|768006797|ref|XP_011524816|]
View 

zinc finger protein 565 isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
6-66 3.95e-34

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.70  E-value: 3.95e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006797     6 VTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASLGLSISKPDVVSLLEQGKEPWM 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-498 2.27e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 193 KPFGCKECGKAFSRASHLVQHQRIHTGEKPYDCKD--CGKAFGRTSELILHQRLHTGVKPYECK---------------- 254
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 255 ECGKTFRQHSQL---------------ILHQRTHTGEKPYvcKDCGKAFIRGSQ-----------------------LTV 296
Cdd:COG5048  112 SSSSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPL--PGNNSSSVNTPQsnslhpplpanslskdpssnlslLIS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 297 HRRIHTGARPYECKECGKAFRQHSQLTVHQRIH------------------------TGEKPYECKECGKGFIHS----- 347
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENsssslplttnsqlspksllsqspsSLSSSDSSSSASESPRSSlptas 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 348 SEVTRHQRIHSGE-----KPYECKECGKAFRQHAQLTRHQR--VHTG--DRPYEC--KDCGKAFSRSSYLIQHQRIHTGD 416
Cdd:COG5048  270 SQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 417 KPYECKEC-------GKAFIRVSQLTHHQRIHTCEKPYEC--RECGMAFIRSSQLTEH--QRIHPGIKPYECRECGQAFI 485
Cdd:COG5048  350 SPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFN 429

                        410
                 ....*....|...
gi 768006797 486 LGSQLIEHYRIHT 498
Cdd:COG5048  430 RHYNLIPHKKIHT 442
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
6-66 3.95e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.70  E-value: 3.95e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006797     6 VTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASLGLSISKPDVVSLLEQGKEPWM 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 5-46 1.49e-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: 87.14  E-value: 1.49e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 768006797    5 LVTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASLG 46
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 6-45 4.78e-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: 80.29  E-value: 4.78e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 768006797   6 VTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASL 45
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-498 2.27e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 193 KPFGCKECGKAFSRASHLVQHQRIHTGEKPYDCKD--CGKAFGRTSELILHQRLHTGVKPYECK---------------- 254
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 255 ECGKTFRQHSQL---------------ILHQRTHTGEKPYvcKDCGKAFIRGSQ-----------------------LTV 296
Cdd:COG5048  112 SSSSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPL--PGNNSSSVNTPQsnslhpplpanslskdpssnlslLIS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 297 HRRIHTGARPYECKECGKAFRQHSQLTVHQRIH------------------------TGEKPYECKECGKGFIHS----- 347
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENsssslplttnsqlspksllsqspsSLSSSDSSSSASESPRSSlptas 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 348 SEVTRHQRIHSGE-----KPYECKECGKAFRQHAQLTRHQR--VHTG--DRPYEC--KDCGKAFSRSSYLIQHQRIHTGD 416
Cdd:COG5048  270 SQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 417 KPYECKEC-------GKAFIRVSQLTHHQRIHTCEKPYEC--RECGMAFIRSSQLTEH--QRIHPGIKPYECRECGQAFI 485
Cdd:COG5048  350 SPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFN 429

                        410
                 ....*....|...
gi 768006797 486 LGSQLIEHYRIHT 498
Cdd:COG5048  430 RHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
405-430 2.97e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.97e-04
                          10        20
                  ....*....|....*....|....*.
gi 768006797  405 YLIQHQRIHTGDKPYECKECGKAFIR 430
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 169-217 1.41e-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: 37.54  E-value: 1.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 768006797 169 CHECGKAFSRGSHLIQHQKIHTgekpFGCKECGKAFSRASHLVQH-QRIH 217
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
6-66 3.95e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.70  E-value: 3.95e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006797     6 VTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASLGLSISKPDVVSLLEQGKEPWM 66
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 5-46 1.49e-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: 87.14  E-value: 1.49e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 768006797    5 LVTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASLG 46
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 6-45 4.78e-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: 80.29  E-value: 4.78e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 768006797   6 VTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASL 45
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-498 2.27e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.20  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 193 KPFGCKECGKAFSRASHLVQHQRIHTGEKPYDCKD--CGKAFGRTSELILHQRLHTGVKPYECK---------------- 254
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 255 ECGKTFRQHSQL---------------ILHQRTHTGEKPYvcKDCGKAFIRGSQ-----------------------LTV 296
Cdd:COG5048  112 SSSSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPL--PGNNSSSVNTPQsnslhpplpanslskdpssnlslLIS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 297 HRRIHTGARPYECKECGKAFRQHSQLTVHQRIH------------------------TGEKPYECKECGKGFIHS----- 347
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENsssslplttnsqlspksllsqspsSLSSSDSSSSASESPRSSlptas 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 348 SEVTRHQRIHSGE-----KPYECKECGKAFRQHAQLTRHQR--VHTG--DRPYEC--KDCGKAFSRSSYLIQHQRIHTGD 416
Cdd:COG5048  270 SQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 417 KPYECKEC-------GKAFIRVSQLTHHQRIHTCEKPYEC--RECGMAFIRSSQLTEH--QRIHPGIKPYECRECGQAFI 485
Cdd:COG5048  350 SPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFN 429

                        410
                 ....*....|...
gi 768006797 486 LGSQLIEHYRIHT 498
Cdd:COG5048  430 RHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-353 1.19e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.72  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 193 KPFGCKECGKAFSRASHLVQHQR--IHTGE--KPYDC--KDCGKAFGRTSELILHQRLHTGVKPYECK--ECGKTFRQ-- 262
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 263 ---HSQLILHQRTHTGEKPYVC--KDCGKAFIRGSQLTVHRRIHTGARPYECK--ECGKAFRQHSQLTVHQRIHTGEKPY 335
Cdd:COG5048  368 nnePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170
                 ....*....|....*...
gi 768006797 336 ECkeCGKGFIHSSEVTRH 353
Cdd:COG5048  448 LC--SILKSFRRDLDLSN 463
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
200-462 3.45e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 3.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 200 CGKAFSRASHLVQHQRIHTGEKPYDCKDCGKAFGRTSeLILHQRLHTGVKPYECKECGKTFRQHSQLILHQRTHTGEKPY 279
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPS-SSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSS 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 280 VCKDCG------KAFIRGSQLTVHRRIHTGAR-PYECKECGKAFRQHSQLTVHQR--IHTGE--KPYECKE--CGKGFIH 346
Cdd:COG5048  256 SASESPrsslptASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSR 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 347 SSEVTRHQRIHSGEKPYECK--ECGKAFRQ-----HAQLTRHQRVHTGDRPYEC--KDCGKAFSRSSYLIQHQRIHTGDK 417
Cdd:COG5048  336 NDALKRHILLHTSISPAKEKllNSSSKFSPllnnePPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFR 415

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768006797 418 PYECK--ECGKAFIRVSQLTHHQRIHTCEKPYECRECGmAFIRSSQL 462
Cdd:COG5048  416 PYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILK-SFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
148-298 9.38e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 9.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 148 FQHHTSHTVRQSRETGEKL--MECHE--CGKAFSRGSHLIQHQKIHTGEKPFGCK--ECGKAFSRASH-----LVQHQRI 216
Cdd:COG5048  301 RSSPLTRHLRSVNHSGESLkpFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNneppqSLQQYKD 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 217 HTGEKPYDC--KDCGKAFGRTSELILHQRLHTGVKPYECK--ECGKTFRQHSQLILHQRTHTGEKPYVCKDCGkaFIRGS 292
Cdd:COG5048  381 LKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILK--SFRRD 458


                 ....*.
gi 768006797 293 QLTVHR 298
Cdd:COG5048  459 LDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
249-499 3.33e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 249 KPYECKECGKTFRQHSQLILHQRTHTGEKPYVCKD--CGKAFIRGSQLTVHRRIHTGARPYECK---------------- 310
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 311 ECGKAFR----QHSQLTVHQRIHTGEKPYE---------CKECGKGFIHSSEVTRHQ----------------------- 354
Cdd:COG5048  112 SSSSNSNdnnlLSSHSLPPSSRDPQLPDLLsisnlrnnpLPGNNSSSVNTPQSNSLHpplpanslskdpssnlsllissn 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006797 355 RIHSGEKPYECKECGKAFRQHAQLTRHQRVHTgDRPYECKDCGKAFSRSSYLIQHQRIHTGDKPYECKECGKAF--IRVS 432
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSlpTASS 270

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006797 433 QLTHHQRIHT-----CEKPYECRECGMAFIRSSQLTEHQR--IH--PGIKPYECRE--CGQAFILGSQLIEHYRIHTG 499
Cdd:COG5048  271 QSSSPNESDSssekgFSLPIKSKQCNISFSRSSPLTRHLRsvNHsgESLKPFSCPYslCGKLFSRNDALKRHILLHTS 348
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
388-442 5.74e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 5.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768006797 388 DRPYECKDCGKAFSRSSYLIQHQRIHTGDKPYEC--KECGKAFIRVSQLTHHQRIHT 442
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHH 87
zf-H2C2_2 pfam13465
Zinc-finger double domain;
405-430 2.97e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.97e-04
                          10        20
                  ....*....|....*....|....*.
gi 768006797  405 YLIQHQRIHTGDKPYECKECGKAFIR 430
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
352-374 4.54e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.54e-04
                          10        20
                  ....*....|....*....|...
gi 768006797  352 RHQRIHSGEKPYECKECGKAFRQ 374
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
378-402 6.92e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.92e-04
                          10        20
                  ....*....|....*....|....*
gi 768006797  378 LTRHQRVHTGDRPYECKDCGKAFSR 402
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
209-232 7.06e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.06e-04
                          10        20
                  ....*....|....*....|....
gi 768006797  209 HLVQHQRIHTGEKPYDCKDCGKAF 232
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-346 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|....*
gi 768006797  322 LTVHQRIHTGEKPYECKECGKGFIH 346
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 169-217 1.41e-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: 37.54  E-value: 1.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 768006797 169 CHECGKAFSRGSHLIQHQKIHTgekpFGCKECGKAFSRASHLVQH-QRIH 217
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 391-413 1.59e-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: 1.59e-03
                          10        20
                  ....*....|....*....|...
gi 768006797  391 YECKDCGKAFSRSSYLIQHQRIH 413
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
416-470 1.70e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 1.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768006797 416 DKPYECKECGKAFIRVSQLTHHQRIHTCEKPYECRECGMA--FIRSSQLTEHQRIHP 470
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 251-273 1.79e-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: 1.79e-03
                          10        20
                  ....*....|....*....|...
gi 768006797  251 YECKECGKTFRQHSQLILHQRTH 273
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
266-290 2.23e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.23e-03
                          10        20
                  ....*....|....*....|....*
gi 768006797  266 LILHQRTHTGEKPYVCKDCGKAFIR 290
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 363-385 2.86e-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: 2.86e-03
                          10        20
                  ....*....|....*....|...
gi 768006797  363 YECKECGKAFRQHAQLTRHQRVH 385
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 307-329 3.04e-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: 3.04e-03
                          10        20
                  ....*....|....*....|...
gi 768006797  307 YECKECGKAFRQHSQLTVHQRIH 329
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
181-206 3.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 768006797  181 HLIQHQKIHTGEKPFGCKECGKAFSR 206
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
237-262 5.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 768006797  237 ELILHQRLHTGVKPYECKECGKTFRQ 262
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 419-441 6.72e-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: 6.72e-03
                          10        20
                  ....*....|....*....|...
gi 768006797  419 YECKECGKAFIRVSQLTHHQRIH 441
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 249-297 8.54e-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: 35.22  E-value: 8.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 768006797 249 KPYeCKECGKTFRQHSQLILHQRTHTgekpYVCKDCGKAFIRGSQLTVH 297
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH