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Conserved domains on  [gi|119577657|gb|EAW57253|]
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zinc finger protein 224, isoform CRA_a [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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 5.31e-22

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 5.31e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119577657     8 MTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVGHQaFHRDTFHFL--REEKIWM 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ-VPKPDLISQleQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
202-639 1.15e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.96  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 202 KCYKCDVCGKEFSQSSHLQTHQRVHTGEKPFKC--VECGKGFSRRSALNVHHKLHTGEKPYNCE-ECGKAFIHDSQLQEH 278
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 279 QRIHTGEKPFKCDICGKSFCGRSRLNRHSMVHTAEKPFRCDTCDKSFRQRSALNSHRMIHTGEkpykcEECGKGFICRRD 358
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLSL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 359 LYTHHMVHTGEKPYNCKECGKSFRWASCLLKHQRVHSgEKPFKCEECGKGFYTNSQCYSHQRSHSgekPYKCVECGKGYK 438
Cdd:COG5048  187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSS---SDSSSSASESPR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 439 RRLDLDFHQR---------VHTGEKL-YNCKECGKSFSRAPCLLKHER--LHSGE--KPFQCEE--CGKRFTQNSHLHSH 502
Cdd:COG5048  263 SSLPTASSQSsspnesdssSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 503 QRVHTGEKPYKC--EKCGKGYNSKFNLDMHQKVHtgerpynckecgksfgwASCLLKHQRLHSGEKPFKCEECGKRFtqN 580
Cdd:COG5048  343 ILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ-----------------QYKDLKNDKKSETLSNSCIRNFKRDS--N 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119577657 581 SQLHSHQRVHTGEKPYKCDECGKGFSWSSTRLTHQRRHSRETPLKCEQHGKNIVQNSFS 639
Cdd:COG5048  404 LSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLS 462
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 5.31e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 5.31e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119577657     8 MTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVGHQaFHRDTFHFL--REEKIWM 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ-VPKPDLISQleQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
8-48 3.49e-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: 86.76  E-value: 3.49e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119577657    8 MTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-46 4.44e-16

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: 72.20  E-value: 4.44e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119577657   8 MTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
202-639 1.15e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.96  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 202 KCYKCDVCGKEFSQSSHLQTHQRVHTGEKPFKC--VECGKGFSRRSALNVHHKLHTGEKPYNCE-ECGKAFIHDSQLQEH 278
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 279 QRIHTGEKPFKCDICGKSFCGRSRLNRHSMVHTAEKPFRCDTCDKSFRQRSALNSHRMIHTGEkpykcEECGKGFICRRD 358
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLSL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 359 LYTHHMVHTGEKPYNCKECGKSFRWASCLLKHQRVHSgEKPFKCEECGKGFYTNSQCYSHQRSHSgekPYKCVECGKGYK 438
Cdd:COG5048  187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSS---SDSSSSASESPR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 439 RRLDLDFHQR---------VHTGEKL-YNCKECGKSFSRAPCLLKHER--LHSGE--KPFQCEE--CGKRFTQNSHLHSH 502
Cdd:COG5048  263 SSLPTASSQSsspnesdssSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 503 QRVHTGEKPYKC--EKCGKGYNSKFNLDMHQKVHtgerpynckecgksfgwASCLLKHQRLHSGEKPFKCEECGKRFtqN 580
Cdd:COG5048  343 ILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ-----------------QYKDLKNDKKSETLSNSCIRNFKRDS--N 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119577657 581 SQLHSHQRVHTGEKPYKCDECGKGFSWSSTRLTHQRRHSRETPLKCEQHGKNIVQNSFS 639
Cdd:COG5048  404 LSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLS 462
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
202-252 5.01e-04

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: 39.46  E-value: 5.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119577657 202 KCYKCDvcgKEFSQSSHLQTHQRvhtgEKPFKCVECGKGFSRRSALNVH----HK 252
Cdd:cd20908    3 WCYYCD---REFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHclqvHK 50
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-297 7.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.25e-04
                          10        20
                  ....*....|....*....|...
gi 119577657  275 LQEHQRIHTGEKPFKCDICGKSF 297
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-67 5.31e-22

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 89.57  E-value: 5.31e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119577657     8 MTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVGHQaFHRDTFHFL--REEKIWM 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ-VPKPDLISQleQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
8-48 3.49e-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: 86.76  E-value: 3.49e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119577657    8 MTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLSVG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-46 4.44e-16

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: 72.20  E-value: 4.44e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119577657   8 MTFKDVAVVFTEEELGLLDLAQRKLYRDVMLENFRNLLS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
202-639 1.15e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 73.96  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 202 KCYKCDVCGKEFSQSSHLQTHQRVHTGEKPFKC--VECGKGFSRRSALNVHHKLHTGEKPYNCE-ECGKAFIHDSQLQEH 278
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 279 QRIHTGEKPFKCDICGKSFCGRSRLNRHSMVHTAEKPFRCDTCDKSFRQRSALNSHRMIHTGEkpykcEECGKGFICRRD 358
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDPSSNLSL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 359 LYTHHMVHTGEKPYNCKECGKSFRWASCLLKHQRVHSgEKPFKCEECGKGFYTNSQCYSHQRSHSgekPYKCVECGKGYK 438
Cdd:COG5048  187 LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSS---SDSSSSASESPR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 439 RRLDLDFHQR---------VHTGEKL-YNCKECGKSFSRAPCLLKHER--LHSGE--KPFQCEE--CGKRFTQNSHLHSH 502
Cdd:COG5048  263 SSLPTASSQSsspnesdssSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 503 QRVHTGEKPYKC--EKCGKGYNSKFNLDMHQKVHtgerpynckecgksfgwASCLLKHQRLHSGEKPFKCEECGKRFtqN 580
Cdd:COG5048  343 ILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ-----------------QYKDLKNDKKSETLSNSCIRNFKRDS--N 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119577657 581 SQLHSHQRVHTGEKPYKCDECGKGFSWSSTRLTHQRRHSRETPLKCEQHGKNIVQNSFS 639
Cdd:COG5048  404 LSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLS 462
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
258-674 2.56e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.09  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 258 KPYNCEECGKAFIHDSQLQEHQRIHTGEKPFKC--DICGKSFCGRSRLNRHSMVHTAEKPFRCDTCDKSFRQRSALNSHR 335
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 336 MIHTGE-KPYKCEECGKGFIcrRDLYTHHMVHTGEKPYNCKE--CGKSFRW-ASCLLKHQRVHSGEKPFKceecgkGFYT 411
Cdd:COG5048  112 SSSSNSnDNNLLSSHSLPPS--SRDPQLPDLLSISNLRNNPLpgNNSSSVNtPQSNSLHPPLPANSLSKD------PSSN 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 412 NSQCYSHQRSHSGEKPYKCVECGKGYKRRLDLDFHQRVHTgEKLYNCKECGKSFSRAPCLLKHERLHSGEKPFQCEECGK 491
Cdd:COG5048  184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 492 RFTQNSHLHSHQRVHTGE-------KPYKCEKCGKGYNSKFNLDMHQ--KVHTGE--RPYNCKE--CGKSFGWASCLLKH 558
Cdd:COG5048  263 SSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 559 QRLHSGEKPFKC--EECGKRFTQNSQLHSHQRvhtgekpykcdecgkgfswsstrlTHQRRHSRETPLKCEQHG---KNI 633
Cdd:COG5048  343 ILLHTSISPAKEklLNSSSKFSPLLNNEPPQS------------------------LQQYKDLKNDKKSETLSNsciRNF 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 119577657 634 VQNSFSEVQEKVHSVEKPYKCED--CGKGYNRRLNLDMHQRVH 674
Cdd:COG5048  399 KRDSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
115-336 1.66e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 115 QDLVINSSQFSKEGDFPCQTEAGLSVIHTRQKSSQGNGYKPSFSDVSHFDFHQQLHSGEKSHTcdecgkNFCYISALRIH 194
Cdd:COG5048  212 PSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSS------PNESDSSSEKG 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 195 QRVHmgekcYKCDVCGKEFSQSSHLQTHQR--VHTGE--KPFKCVE--CGKGFSRRSALNVHHKLHTGEKPYNC--EECG 266
Cdd:COG5048  286 FSLP-----IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSS 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 267 KAFIHDS------QLQEHQRIHT-------------------------------GEKPFKCDICGKSFCGRSRLNRHSMV 309
Cdd:COG5048  361 SKFSPLLnneppqSLQQYKDLKNdkksetlsnscirnfkrdsnlslhiithlsfRPYNCKNPPCSKSFNRHYNLIPHKKI 440
                        250       260
                 ....*....|....*....|....*..
gi 119577657 310 HTAEKPFRCDTCDKSFRQRSALNSHRM 336
Cdd:COG5048  441 HTNHAPLLCSILKSFRRDLDLSNHGKD 467
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
508-591 1.83e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 508 GEKPYKCE--KCGKGYNSKFNLDMHQKvHtgerpyncKECGKSFGWASCLLKHQRLHSGEKPFKCEECGKRFTQNSQLHS 585
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 119577657 586 HqRVHT 591
Cdd:COG5189  417 H-RKHS 421
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
424-507 2.16e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.41  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 424 GEKPYKC--VECGKGYKRRLDLDFHqRVHtgeklyncKECGKSFSRAPCLLKHERLHSGEKPFQCEECGKRFTQNSHLHS 501
Cdd:COG5189  346 DGKPYKCpvEGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 119577657 502 HqRVHT 507
Cdd:COG5189  417 H-RKHS 421
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
213-351 2.52e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 213 FSQSSHLQTHQRVHtgeKPFKCVECGKGFSRRSALNVHhklhtgEKPYNCEECGKAFIHDSQLQ---EHQRIHT-GEKPF 288
Cdd:COG5189  280 FEESSLGFDYEFIH---KSVGNKEIRGGISTGEMIDVR------KLPCTNSSSNGKLAHGGERNidtPSRMLKVkDGKPY 350
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119577657 289 KCDI--CGKSFCGRSRLNRHsMVHTAEKPFRCDTCDKsfrqrsalNSHRMIHTGEKPYKCEECGK 351
Cdd:COG5189  351 KCPVegCNKKYKNQNGLKYH-MLHGHQNQKLHENPSP--------EKMNIFSAKDKPYRCEVCDK 406
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
202-252 5.01e-04

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: 39.46  E-value: 5.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119577657 202 KCYKCDvcgKEFSQSSHLQTHQRvhtgEKPFKCVECGKGFSRRSALNVH----HK 252
Cdd:cd20908    3 WCYYCD---REFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHclqvHK 50
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-297 7.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.25e-04
                          10        20
                  ....*....|....*....|...
gi 119577657  275 LQEHQRIHTGEKPFKCDICGKSF 297
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
565-674 1.82e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119577657 565 EKPFKCEECGKRFTQNSQLH----SHQRVHTGEKPYKCD--ECGKGFSwSSTRLTHQRRHSRETPlKCEQHGKNIVQNSF 638
Cdd:COG5189  315 KLPCTNSSSNGKLAHGGERNidtpSRMLKVKDGKPYKCPveGCNKKYK-NQNGLKYHMLHGHQNQ-KLHENPSPEKMNIF 392
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119577657 639 SevqekvhSVEKPYKCEDCGKGYNRRLNLDMHqRVH 674
Cdd:COG5189  393 S-------AKDKPYRCEVCDKRYKNLNGLKYH-RKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
555-579 4.16e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.16e-03
                          10        20
                  ....*....|....*....|....*
gi 119577657  555 LLKHQRLHSGEKPFKCEECGKRFTQ 579
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-549 4.87e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.87e-03
                          10        20
                  ....*....|....*....|....
gi 119577657  526 NLDMHQKVHTGERPYNCKECGKSF 549
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
471-495 5.87e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.87e-03
                          10        20
                  ....*....|....*....|....*
gi 119577657  471 LLKHERLHSGEKPFQCEECGKRFTQ 495
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
204-226 6.26e-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: 6.26e-03
                          10        20
                  ....*....|....*....|...
gi 119577657  204 YKCDVCGKEFSQSSHLQTHQRVH 226
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
330-355 7.29e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 7.29e-03
                          10        20
                  ....*....|....*....|....*.
gi 119577657  330 ALNSHRMIHTGEKPYKCEECGKGFIC 355
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
484-506 7.69e-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: 7.69e-03
                          10        20
                  ....*....|....*....|...
gi 119577657  484 FQCEECGKRFTQNSHLHSHQRVH 506
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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