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Conserved domains on  [gi|1907092982|ref|XP_036013812|]
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zinc finger protein 184 isoform X2 [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016931)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-68 4.30e-20

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: 83.67  E-value: 4.30e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907092982  27 SVTFKDVVVNFTQEEWKHLDPIQRDLFRDVTLENYTHLVSID 68
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
131-602 2.72e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.81  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 131 SNLSVSSSFITQTEVALDQPSTKTRAKQNshpvkKEKLCKCNECGKAFTYCSALIRHQRTHTGEKPYKCN--ECNKAFSR 208
Cdd:COG5048     1 ATLTSSQSSSSNNSVLSSTPKSTLKSLSN-----APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 209 SENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIHTGE-KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCTECG 287
Cdd:COG5048    76 PLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 288 KSFSqrgHFMEHQKIHtGEKPFKCEECEKTFTRSTHLtqHQKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYEC 367
Cdd:COG5048   156 SSSV---NTPQSNSLH-PPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 368 NECGKAFSQHSNLTQHQKTHTGEKPydcaecgkafSYWSSLAQHLKIHTGEKPYKcsdcgkafSYCSSLTQHRRIHTREK 447
Cdd:COG5048   230 TTNSQLSPKSLLSQSPSSLSSSDSS----------SSASESPRSSLPTASSQSSS--------PNESDSSSEKGFSLPIK 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 448 pfeCSECGKAFSYLSNLNQHQKT--HTQE--KAYECKE--CGKAFIRSSSLAKHERIHTGEKPYQCHECGKTFSYGSSL- 520
Cdd:COG5048   292 ---SKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLn 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 521 ------IQHKKIHTGERPYKC--NECGRAFNQKIHLTQHKRIHTGAKPYAC--PKCGKTFRHCSSLAQHQKTHTEEKPYQ 590
Cdd:COG5048   369 neppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLL 448

                         490
                  ....*....|..
gi 1907092982 591 CNKCEKTFSQNS 602
Cdd:COG5048   449 CSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
603-627 9.52e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.52e-04
                          10        20
                  ....*....|....*....|....*
gi 1907092982 603 RLTQHQRIHTGEKPYKCSECDKCFT 627
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-68 4.30e-20

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: 83.67  E-value: 4.30e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907092982  27 SVTFKDVVVNFTQEEWKHLDPIQRDLFRDVTLENYTHLVSID 68
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
28-81 1.38e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 82.64  E-value: 1.38e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907092982   28 VTFKDVVVNFTQEEWKHLDPIQRDLFRDVTLENYTHLVSIDWKKRAGNSVSSLE 81
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 28-67 5.14e-18

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: 77.59  E-value: 5.14e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907092982  28 VTFKDVVVNFTQEEWKHLDPIQRDLFRDVTLENYTHLVSI 67
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
131-602 2.72e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.81  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 131 SNLSVSSSFITQTEVALDQPSTKTRAKQNshpvkKEKLCKCNECGKAFTYCSALIRHQRTHTGEKPYKCN--ECNKAFSR 208
Cdd:COG5048     1 ATLTSSQSSSSNNSVLSSTPKSTLKSLSN-----APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 209 SENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIHTGE-KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCTECG 287
Cdd:COG5048    76 PLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 288 KSFSqrgHFMEHQKIHtGEKPFKCEECEKTFTRSTHLtqHQKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYEC 367
Cdd:COG5048   156 SSSV---NTPQSNSLH-PPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 368 NECGKAFSQHSNLTQHQKTHTGEKPydcaecgkafSYWSSLAQHLKIHTGEKPYKcsdcgkafSYCSSLTQHRRIHTREK 447
Cdd:COG5048   230 TTNSQLSPKSLLSQSPSSLSSSDSS----------SSASESPRSSLPTASSQSSS--------PNESDSSSEKGFSLPIK 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 448 pfeCSECGKAFSYLSNLNQHQKT--HTQE--KAYECKE--CGKAFIRSSSLAKHERIHTGEKPYQCHECGKTFSYGSSL- 520
Cdd:COG5048   292 ---SKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLn 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 521 ------IQHKKIHTGERPYKC--NECGRAFNQKIHLTQHKRIHTGAKPYAC--PKCGKTFRHCSSLAQHQKTHTEEKPYQ 590
Cdd:COG5048   369 neppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLL 448

                         490
                  ....*....|..
gi 1907092982 591 CNKCEKTFSQNS 602
Cdd:COG5048   449 CSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-264 1.69e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.69e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 239 SLTQHQRIHTGEKPYKCDECGKAFSQ 264
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
603-627 9.52e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.52e-04
                          10        20
                  ....*....|....*....|....*
gi 1907092982 603 RLTQHQRIHTGEKPYKCSECDKCFT 627
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 307-347 3.15e-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: 37.15  E-value: 3.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907092982 307 KPFkCEECEKTFTRSTHLTQHQKihtgEKTYKCNECGKAFN 347
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLY 36
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-68 4.30e-20

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: 83.67  E-value: 4.30e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907092982  27 SVTFKDVVVNFTQEEWKHLDPIQRDLFRDVTLENYTHLVSID 68
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
28-81 1.38e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 82.64  E-value: 1.38e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907092982   28 VTFKDVVVNFTQEEWKHLDPIQRDLFRDVTLENYTHLVSIDWKKRAGNSVSSLE 81
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 28-67 5.14e-18

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: 77.59  E-value: 5.14e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907092982  28 VTFKDVVVNFTQEEWKHLDPIQRDLFRDVTLENYTHLVSI 67
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
131-602 2.72e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 72.81  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 131 SNLSVSSSFITQTEVALDQPSTKTRAKQNshpvkKEKLCKCNECGKAFTYCSALIRHQRTHTGEKPYKCN--ECNKAFSR 208
Cdd:COG5048     1 ATLTSSQSSSSNNSVLSSTPKSTLKSLSN-----APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 209 SENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIHTGE-KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCTECG 287
Cdd:COG5048    76 PLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 288 KSFSqrgHFMEHQKIHtGEKPFKCEECEKTFTRSTHLtqHQKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYEC 367
Cdd:COG5048   156 SSSV---NTPQSNSLH-PPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 368 NECGKAFSQHSNLTQHQKTHTGEKPydcaecgkafSYWSSLAQHLKIHTGEKPYKcsdcgkafSYCSSLTQHRRIHTREK 447
Cdd:COG5048   230 TTNSQLSPKSLLSQSPSSLSSSDSS----------SSASESPRSSLPTASSQSSS--------PNESDSSSEKGFSLPIK 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 448 pfeCSECGKAFSYLSNLNQHQKT--HTQE--KAYECKE--CGKAFIRSSSLAKHERIHTGEKPYQCHECGKTFSYGSSL- 520
Cdd:COG5048   292 ---SKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLn 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 521 ------IQHKKIHTGERPYKC--NECGRAFNQKIHLTQHKRIHTGAKPYAC--PKCGKTFRHCSSLAQHQKTHTEEKPYQ 590
Cdd:COG5048   369 neppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLL 448

                         490
                  ....*....|..
gi 1907092982 591 CNKCEKTFSQNS 602
Cdd:COG5048   449 CSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
251-656 7.71e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 7.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 251 KPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCT--ECGKSFSQRGHFMEHQKIHTGEKPFKCEECEKTFTRST-HLTQH 327
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAsSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 328 QKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHT---GEKPYECNECGKAFSQhSNLTQHQKTHTgekpydcAECGKAFSY 404
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQ-SNSLHPPLPAN-------SLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 405 WSSLAQHLKIHTGEKPYKCSDCGKAFSYcSSLTQHRRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKECG- 483
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSI-PSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPr 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 484 -----KAFIRSSSLAKHERIHTG-EKPYQCHECGKTFSYGSSLIQHK--KIHTGE--RPYKCNE--CGRAFNQKIHLTQH 551
Cdd:COG5048   263 sslptASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 552 KRIHTGAKPYACP--KCGKTFRHCS-----SLAQHQKTHTEEKPYQC--NKCEKTFSQNSRLTQHQRIHTGEKP--YKCS 620
Cdd:COG5048   343 ILLHTSISPAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1907092982 621 ECDKCFTGSVHLTEHRSTHTGEKPYNSECPQTFSQS 656
Cdd:COG5048   423 PCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
307-683 6.47e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 307 KPFKCEECEKTFTRSTHLTQHQKIHTGEKTYKCN--ECGKAFNGPSTFIRHHMIHTGEKPYECN-ECGKAFSQHSNLTQH 383
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 384 QKTHTGEKPYDCAECGKAFSYWSSLAQHLKIHTGEKPYKCSDCGKAF----------------------SYCSSLTQHRR 441
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSvntpqsnslhpplpanslskdpSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 442 IHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKECGKAFIRSSSLAKHERIHTGEKPYQCHECGKTFSYGSSLI 521
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQ 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 522 QHKKIHTGER-------PYKCNECGRAFNQKIHLTQHKR--IHTG--AKPYACPK--CGKTFRHCSSLAQHQKTHTEEKP 588
Cdd:COG5048   272 SSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 589 YQC--NKCEKTFSQ--NSRLTQHQRIHTGEKPYKCSECD-----KCFTGSVHLTEHRSTHTGEKPYN---SECPQTFSQS 656
Cdd:COG5048   352 AKEklLNSSSKFSPllNNEPPQSLQQYKDLKNDKKSETLsnsciRNFKRDSNLSLHIITHLSFRPYNcknPPCSKSFNRH 431

                         410       420
                  ....*....|....*....|....*..
gi 1907092982 657 TYLTQHQKIHSGEKLLGCEDCEKAFQC 683
Cdd:COG5048   432 YNLIPHKKIHTNHAPLLCSILKSFRRD 458
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
114-356 1.90e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 114 MLPREVQITEKTAPTCESNLSVSSSFITQTE---VALDQPSTKTRAKQNSHPVKKEKL----CKCNECGKAFTYCSALIR 186
Cdd:COG5048   228 PLTTNSQLSPKSLLSQSPSSLSSSDSSSSASespRSSLPTASSQSSSPNESDSSSEKGfslpIKSKQCNISFSRSSPLTR 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 187 HQRT--HTGE--KPYKCNE--CNKAFSRSENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQhqrihtgekpykcdecgk 260
Cdd:COG5048   308 HLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN------------------ 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 261 afSQRTHLVQHQRIHTGEKPYTCTECGKSFSQRGHFMEHQKIHT---GEKPFKCEECEKTFTRSTHLTQHQKIHTgEKTY 337
Cdd:COG5048   370 --EPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHlsfRPYNCKNPPCSKSFNRHYNLIPHKKIHT-NHAP 446

                         250
                  ....*....|....*....
gi 1907092982 338 KCNECGKAFNGPSTFIRHH 356
Cdd:COG5048   447 LLCSILKSFRRDLDLSNHG 465
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-264 1.69e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.69e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 239 SLTQHQRIHTGEKPYKCDECGKAFSQ 264
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
267-292 2.87e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.87e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 267 HLVQHQRIHTGEKPYTCTECGKSFSQ 292
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
491-516 4.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.93e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 491 SLAKHERIHTGEKPYQCHECGKTFSY 516
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
183-208 5.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.18e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 183 ALIRHQRTHTGEKPYKCNECNKAFSR 208
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
407-432 5.55e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.55e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 407 SLAQHLKIHTGEKPYKCSDCGKAFSY 432
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
603-627 9.52e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.52e-04
                          10        20
                  ....*....|....*....|....*
gi 1907092982 603 RLTQHQRIHTGEKPYKCSECDKCFT 627
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
295-320 1.04e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 295 HFMEHQKIHTGEKPFKCEECEKTFTR 320
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
379-404 1.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 379 NLTQHQKTHTGEKPYDCAECGKAFSY 404
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 193-271 1.50e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 193 GEKPYKCN--ECNKAFsRSENLINHQRIHtgdkpykcDQCGKGFIEGPSLTQHQRIHTGEKPYKCDECGKAFSQRTHLVQ 270
Cdd:COG5189   346 DGKPYKCPveGCNKKY-KNQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  .
gi 1907092982 271 H 271
Cdd:COG5189   417 H 417
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 305-388 1.70e-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: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907092982 305 GEKPFKCE--ECEKTFTRSTHLTQHQKI-HTGEKTYKcnecgkafnGPSTfIRHHMIHTGEKPYECNECGKAFSQHSNLT 381
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMLHgHQNQKLHE---------NPSP-EKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                  ....*..
gi 1907092982 382 QHQKTHT 388
Cdd:COG5189   416 YHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
463-488 2.05e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 463 NLNQHQKTHTQEKAYECKECGKAFIR 488
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
519-544 2.05e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 519 SLIQHKKIHTGERPYKCNECGRAFNQ 544
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
323-347 2.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.62e-03
                          10        20
                  ....*....|....*....|....*
gi 1907092982 323 HLTQHQKIHTGEKTYKCNECGKAFN 347
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
211-234 2.78e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.78e-03
                          10        20
                  ....*....|....*....|....
gi 1907092982 211 NLINHQRIHTGDKPYKCDQCGKGF 234
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
547-572 3.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.09e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 547 HLTQHKRIHTGAKPYACPKCGKTFRH 572
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 307-347 3.15e-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: 37.15  E-value: 3.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907092982 307 KPFkCEECEKTFTRSTHLTQHQKihtgEKTYKCNECGKAFN 347
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLY 36
zf-H2C2_2 pfam13465
Zinc-finger double domain;
435-460 3.35e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.35e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 435 SLTQHRRIHTREKPFECSECGKAFSY 460
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 365-387 5.49e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 5.49e-03
                          10        20
                  ....*....|....*....|...
gi 1907092982 365 YECNECGKAFSQHSNLTQHQKTH 387
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
575-600 5.97e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.97e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907092982 575 SLAQHQKTHTEEKPYQCNKCEKTFSQ 600
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 197-219 7.30e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 7.30e-03
                          10        20
                  ....*....|....*....|...
gi 1907092982 197 YKCNECNKAFSRSENLINHQRIH 219
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
354-376 7.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 7.42e-03
                          10        20
                  ....*....|....*....|...
gi 1907092982 354 RHHMIHTGEKPYECNECGKAFSQ 376
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
 
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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