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Conserved domains on  [gi|530409060|ref|XP_005255615|]
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transcriptional repressor RHIT isoform X1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204351)

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

Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  22803940|14519192|8183940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
124-168 2.24e-15

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 70.70  E-value: 2.24e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530409060   124 VTFEDVALYLSREEWGRLDHTQQNFYRDVLQK--KNGLSLGFPFSRP 168
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLEnySNLVSLGFQVPKP 47
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-486 4.42e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 4.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 306 KSYRCEQCGKGFSWHSHLVTHRRT--HTGE--KPYACT--DCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSH---- 375
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 376 ---HSTLIQHQRIHTGEKPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPicakcftqssalvthqrthtgvkpypC 450
Cdd:COG5048  368 nnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------N 421

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530409060 451 PECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFS 486
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 476-498 5.11e-05

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: 40.36  E-value: 5.11e-05
                          10        20
                  ....*....|....*....|...
gi 530409060  476 YHCLDCGKSFSHSSHLTAHQRTH 498
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 504-526 2.89e-04

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 2.89e-04
                          10        20
                  ....*....|....*....|...
gi 530409060  504 YACPLCGKSFSRRSNLHRHEKIH 526
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
124-168 2.24e-15

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 70.70  E-value: 2.24e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530409060   124 VTFEDVALYLSREEWGRLDHTQQNFYRDVLQK--KNGLSLGFPFSRP 168
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLEnySNLVSLGFQVPKP 47
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 124-158 2.52e-13

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: 64.11  E-value: 2.52e-13
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 530409060 124 VTFEDVALYLSREEWGRLDHTQQNFYRDVLQKKNG 158
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYE 35
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 123-162 2.50e-12

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: 61.33  E-value: 2.50e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 530409060  123 PVTFEDVALYLSREEWGRLDHTQQNFYRDVLQ--KKNGLSLG 162
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLenYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-486 4.42e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 4.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 306 KSYRCEQCGKGFSWHSHLVTHRRT--HTGE--KPYACT--DCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSH---- 375
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 376 ---HSTLIQHQRIHTGEKPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPicakcftqssalvthqrthtgvkpypC 450
Cdd:COG5048  368 nnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------N 421

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530409060 451 PECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFS 486
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
434-459 2.92e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.92e-05
                          10        20
                  ....*....|....*....|....*.
gi 530409060  434 ALVTHQRTHTGVKPYPCPECGKCFSQ 459
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 476-498 5.11e-05

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: 40.36  E-value: 5.11e-05
                          10        20
                  ....*....|....*....|...
gi 530409060  476 YHCLDCGKSFSHSSHLTAHQRTH 498
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 504-526 2.89e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 2.89e-04
                          10        20
                  ....*....|....*....|...
gi 530409060  504 YACPLCGKSFSRRSNLHRHEKIH 526
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 363-410 5.79e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.24  E-value: 5.79e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530409060 363 PYTCPACRKSFSHHSTLIQHQRIHTGEKpyVCDRCAKRFTRRSDLVTH 410
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 362-410 9.17e-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: 38.31  E-value: 9.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530409060 362 KPYtCPACRKSFSHHSTLIQHQRIHTgekpYVCDRCAKRFTRRSDLVTH 410
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
124-168 2.24e-15

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 70.70  E-value: 2.24e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530409060   124 VTFEDVALYLSREEWGRLDHTQQNFYRDVLQK--KNGLSLGFPFSRP 168
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLEnySNLVSLGFQVPKP 47
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 124-158 2.52e-13

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: 64.11  E-value: 2.52e-13
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 530409060 124 VTFEDVALYLSREEWGRLDHTQQNFYRDVLQKKNG 158
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYE 35
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 123-162 2.50e-12

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: 61.33  E-value: 2.50e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 530409060  123 PVTFEDVALYLSREEWGRLDHTQQNFYRDVLQ--KKNGLSLG 162
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLenYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-486 4.42e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 4.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 306 KSYRCEQCGKGFSWHSHLVTHRRT--HTGE--KPYACT--DCGKRFGRSSHLIQHQIIHTGEKPYTCPACRKSFSH---- 375
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 376 ---HSTLIQHQRIHTGEKPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPicakcftqssalvthqrthtgvkpypC 450
Cdd:COG5048  368 nnePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCK--------------------------N 421

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530409060 451 PECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFS 486
Cdd:COG5048  422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-528 4.67e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 4.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 369 CRKSFSHHSTLiQHQRIHTgekPYVCDRCAKRFTRRSDLVTHQGT--HTG--AKPHKCPI--CAKCFTQSSALVTHQRTH 442
Cdd:COG5048  271 QSSSPNESDSS-SEKGFSL---PIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 443 TGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD---------CGKSFSHSSHLTAHQRTHRGVRPYAC--PLCGK 511
Cdd:COG5048  347 TSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDkksetlsnsCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSK 426

                        170
                 ....*....|....*..
gi 530409060 512 SFSRRSNLHRHEKIHTT 528
Cdd:COG5048  427 SFNRHYNLIPHKKIHTN 443
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
362-523 5.52e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.72  E-value: 5.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 362 KPYTCPACRKSFSHHSTLIQHQR--IHTGE--KPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPICAKCFTQSSAL 435
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 436 VT-------HQRTHTGVKPYPC--PECGKCFSQRSNLIAHNRTHTGEKPYHC--LDCGKSFSHSSHLTAHQRTHRGVRPY 504
Cdd:COG5048  368 NNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170
                 ....*....|....*....
gi 530409060 505 ACPLCGKSFSRRSNLHRHE 523
Cdd:COG5048  448 LCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
341-526 1.37e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 341 CGKRFGRSSHLIQHQIIHTGeKPYTCPACRKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPH 420
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSI-PSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSS 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 421 KCPICAKCFTQSSALVTHQRTHTGV-------KPYPCPECGKCFSQRSNLIAHNRT--HTGE--KPYHC--LDCGKSFSH 487
Cdd:COG5048  256 SASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSR 335

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530409060 488 SSHLTAHQRTHRGVRPYACPL--CGKSFSRRSNLHRHEKIH 526
Cdd:COG5048  336 NDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
306-527 2.64e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.71  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 306 KSYRCEQCGKGFSWHSHLVTHRRTHTGEKPYACTD--CGKRFGRSSHLIQHQIIHTGEKPYTCPACRKS----------- 372
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 373 ---------------------------FSHHSTLIQHQRIHTGEKPYVCDRCA-------------KRFTRRSDLVTHQG 412
Cdd:COG5048  112 ssssnsndnnllsshslppssrdpqlpDLLSISNLRNNPLPGNNSSSVNTPQSnslhpplpanslsKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 413 THTGAKPHKCPICAKCFTQSSALVTHQRTHTGVKPYPCPECGKCFSQRSNL------------------IAHNRTHTGE- 473
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSqspsslsssdssssasesPRSSLPTASSq 271

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530409060 474 ----------------KPYHCLDCGKSFSHSSHLTAHQRTH----RGVRPYACP--LCGKSFSRRSNLHRHEKIHT 527
Cdd:COG5048  272 ssspnesdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSVnhsgESLKPFSCPysLCGKLFSRNDALKRHILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
430-498 6.08e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 6.08e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530409060 430 TQSSALVTHQRTHTGV----KPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD--CGKSFSHSSHLTAHQRTH 498
Cdd:COG5048   12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
zf-H2C2_2 pfam13465
Zinc-finger double domain;
434-459 2.92e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.92e-05
                          10        20
                  ....*....|....*....|....*.
gi 530409060  434 ALVTHQRTHTGVKPYPCPECGKCFSQ 459
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 476-498 5.11e-05

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: 40.36  E-value: 5.11e-05
                          10        20
                  ....*....|....*....|...
gi 530409060  476 YHCLDCGKSFSHSSHLTAHQRTH 498
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
350-375 7.72e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 7.72e-05
                          10        20
                  ....*....|....*....|....*.
gi 530409060  350 HLIQHQIIHTGEKPYTCPACRKSFSH 375
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-345 1.19e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.19e-04
                          10        20
                  ....*....|....*....|....
gi 530409060  322 HLVTHRRTHTGEKPYACTDCGKRF 345
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 448-470 1.47e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.82  E-value: 1.47e-04
                          10        20
                  ....*....|....*....|...
gi 530409060  448 YPCPECGKCFSQRSNLIAHNRTH 470
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
462-487 1.94e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.94e-04
                          10        20
                  ....*....|....*....|....*.
gi 530409060  462 NLIAHNRTHTGEKPYHCLDCGKSFSH 487
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 504-526 2.89e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 2.89e-04
                          10        20
                  ....*....|....*....|...
gi 530409060  504 YACPLCGKSFSRRSNLHRHEKIH 526
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-515 3.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.78e-04
                          10        20
                  ....*....|....*....|....*.
gi 530409060  490 HLTAHQRTHRGVRPYACPLCGKSFSR 515
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 363-410 5.79e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 40.24  E-value: 5.79e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530409060 363 PYTCPACRKSFSHHSTLIQHQRIHTGEKpyVCDRCAKRFTRRSDLVTH 410
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
379-403 8.45e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.45e-04
                          10        20
                  ....*....|....*....|....*
gi 530409060  379 LIQHQRIHTGEKPYVCDRCAKRFTR 403
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 362-410 9.17e-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: 38.31  E-value: 9.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530409060 362 KPYtCPACRKSFSHHSTLIQHQRIHTgekpYVCDRCAKRFTRRSDLVTH 410
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 360-443 1.15e-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: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 360 GEKPYTCP--ACRKSFSHHSTLIQHqRIHtgekpyvcDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICAKCFTQSSALVT 437
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 530409060 438 HqRTHT 443
Cdd:COG5189  417 H-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 420-442 1.43e-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: 36.12  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|...
gi 530409060  420 HKCPICAKCFTQSSALVTHQRTH 442
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 336-358 2.10e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.10e-03
                          10        20
                  ....*....|....*....|...
gi 530409060  336 YACTDCGKRFGRSSHLIQHQIIH 358
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 416-498 2.25e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409060 416 GAKPHKCPI--CAKCFTQSSALVTHQRT-HTGVKPYPCPecgkcfsqrsNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLT 492
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYHMLHgHQNQKLHENP----------SPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                 ....*.
gi 530409060 493 AHqRTH 498
Cdd:COG5189  416 YH-RKH 420
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 364-386 3.67e-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: 3.67e-03
                          10        20
                  ....*....|....*....|...
gi 530409060  364 YTCPACRKSFSHHSTLIQHQRIH 386
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 419-466 5.37e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 5.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530409060 419 PHKCPICAKCFTQSSALVTHQR--THTGVkpypCPECGKCFSQRSNLIAH 466
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKV----CPVCGKEFRNTDSTLDH 118
 
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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