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Conserved domains on  [gi|1720389932|ref|XP_030105610|]
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transcriptional repressor Rhit isoform X4 [Mus musculus]

Protein Classification

KRAB_A-box and COG5048 domain-containing protein( domain architecture ID 11577774)

protein containing domains KRAB_A-box, zf-H2C2_2, and COG5048

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
117-151 1.27e-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: 64.88  E-value: 1.27e-13
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720389932 117 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQGKNG 151
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYE 35
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
336-496 1.55e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 336 SCWKSFSHHSTLiQHQRIHTgekPYVCDRCAKRFTRRSDLVTHQGT--HTG--AKPHKCPI--CSKCFTQSSALVTHQRT 409
Cdd:COG5048   270 SQSSSPNESDSS-SEKGFSL---PIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILL 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 410 HTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD---------CGKSFSHSSHLTAHQRTHRGVRPYSC--PLCG 478
Cdd:COG5048   346 HTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDkksetlsnsCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425
                         170
                  ....*....|....*...
gi 1720389932 479 KSFSRRSNLHRHEKIHTT 496
Cdd:COG5048   426 KSFNRHYNLIPHKKIHTN 443
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-313 1.40e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.40e-04
                          10        20
                  ....*....|....*....|....
gi 1720389932 290 HLVTHRRTHTGEKPYTCTDCGKRF 313
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
304-326 1.10e-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: 36.51  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|...
gi 1720389932 304 YTCTDCGKRFGRSSHLIQHQIIH 326
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
117-151 1.27e-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: 64.88  E-value: 1.27e-13
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720389932 117 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQGKNG 151
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYE 35
KRAB smart00349
krueppel associated box;
117-165 1.32e-13

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 65.31  E-value: 1.32e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720389932  117 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQ--GKN--GLALALPSPEVYRQL 165
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLenYSNlvSLGFQVPKPDLISQL 53
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
116-147 2.34e-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: 2.34e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720389932 116 PVTFEDVALYLSQEEWGRLDHTQQNFYRDVLQ 147
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVML 32
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
336-496 1.55e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 336 SCWKSFSHHSTLiQHQRIHTgekPYVCDRCAKRFTRRSDLVTHQGT--HTG--AKPHKCPI--CSKCFTQSSALVTHQRT 409
Cdd:COG5048   270 SQSSSPNESDSS-SEKGFSL---PIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILL 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 410 HTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD---------CGKSFSHSSHLTAHQRTHRGVRPYSC--PLCG 478
Cdd:COG5048   346 HTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDkksetlsnsCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425
                         170
                  ....*....|....*...
gi 1720389932 479 KSFSRRSNLHRHEKIHTT 496
Cdd:COG5048   426 KSFNRHYNLIPHKKIHTN 443
zf-H2C2_2 pfam13465
Zinc-finger double domain;
402-427 3.96e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.96e-05
                          10        20
                  ....*....|....*....|....*.
gi 1720389932 402 ALVTHQRTHTGVKPYPCPECGKCFSQ 427
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-313 1.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.40e-04
                          10        20
                  ....*....|....*....|....
gi 1720389932 290 HLVTHRRTHTGEKPYTCTDCGKRF 313
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
304-326 1.10e-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: 36.51  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|...
gi 1720389932 304 YTCTDCGKRFGRSSHLIQHQIIH 326
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
331-378 1.43e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.70  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720389932 331 PYTCPSCWKSFSHHSTLIQHQRIHTGEKpyVCDRCAKRFTRRSDLVTH 378
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
335-378 2.99e-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: 36.77  E-value: 2.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720389932 335 PSCW---KSFSHHSTLIQHQRIHTgekpYVCDRCAKRFTRRSDLVTH 378
Cdd:cd20908     2 PWCYycdREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
117-151 1.27e-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: 64.88  E-value: 1.27e-13
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720389932 117 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQGKNG 151
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYE 35
KRAB smart00349
krueppel associated box;
117-165 1.32e-13

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 65.31  E-value: 1.32e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720389932  117 VTFEDVALYLSQEEWGRLDHTQQNFYRDVLQ--GKN--GLALALPSPEVYRQL 165
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLenYSNlvSLGFQVPKPDLISQL 53
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
116-147 2.34e-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: 2.34e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720389932 116 PVTFEDVALYLSQEEWGRLDHTQQNFYRDVLQ 147
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVML 32
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
336-496 1.55e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 336 SCWKSFSHHSTLiQHQRIHTgekPYVCDRCAKRFTRRSDLVTHQGT--HTG--AKPHKCPI--CSKCFTQSSALVTHQRT 409
Cdd:COG5048   270 SQSSSPNESDSS-SEKGFSL---PIKSKQCNISFSRSSPLTRHLRSvnHSGesLKPFSCPYslCGKLFSRNDALKRHILL 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 410 HTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD---------CGKSFSHSSHLTAHQRTHRGVRPYSC--PLCG 478
Cdd:COG5048   346 HTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDkksetlsnsCIRNFKRDSNLSLHIITHLSFRPYNCknPPCS 425
                         170
                  ....*....|....*...
gi 1720389932 479 KSFSRRSNLHRHEKIHTT 496
Cdd:COG5048   426 KSFNRHYNLIPHKKIHTN 443
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
330-491 1.74e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 330 KPYTCPSCWKSFSHHSTLIQHQR--IHTGE--KPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPHKCPICSKCFTQSSAL 403
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 404 VT-------HQRTHTGVKPYPC--PECGKCFSQRSNLIAHNRTHTGEKPYHC--LDCGKSFSHSSHLTAHQRTHRGVRPY 472
Cdd:COG5048   368 NNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPL 447
                         170
                  ....*....|....*....
gi 1720389932 473 SCPLCGKSFSRRSNLHRHE 491
Cdd:COG5048   448 LCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
276-436 3.28e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.41  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 276 YKCEQCGKGFSWHSHLVTHRRT--HTGE--KPYTCT--DCGKRFGRSSHLIQHQIIHTGEKPYTCPSCWKSFSH------ 343
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnn 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 344 -HSTLIQHQRIHTGEKPYVCD--RCAKRFTRRSDLVTHQGTHTGAKPH--KCPICSKCFTQSSALVTHQRTHTgVKPYPC 418
Cdd:COG5048   370 ePPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHT-NHAPLL 448
                         170
                  ....*....|....*...
gi 1720389932 419 PECGKCFSQRSNLIAHNR 436
Cdd:COG5048   449 CSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
283-454 3.51e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 283 KGFSWHSHLVTHRRTHTG-EKPYTCTDCGKRFGRSSHLIQHQ--IIHTGE--KPYTCPS--CWKSFSHHSTLIQHQRIHT 355
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 356 GEKPYVC--DRCAKRFT------RRSDLVTHQGTHTGaKPHKC--PICSKCFTQSSALVTHQRTHTGVKP--YPCPECGK 423
Cdd:COG5048   348 SISPAKEklLNSSSKFSpllnnePPQSLQQYKDLKND-KKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSK 426
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720389932 424 CFSQRSNLIAHNRTHTGEKPYHCLDCGKSFS 454
Cdd:COG5048   427 SFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-495 3.67e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 273 KKTYKCEQCGKGFSWHSHLVTHRRTHTGEKPYTCTD--CGKRFGRSSHLIQHQIIHTGEKPYTCP--------------- 335
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkslplsnskassssl 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 336 --SCWKSFSH---------------------HSTLIQHQRIHTGEKPYVCDRCA-------------KRFTRRSDLVTHQ 379
Cdd:COG5048   111 ssSSSNSNDNnllsshslppssrdpqlpdllSISNLRNNPLPGNNSSSVNTPQSnslhpplpanslsKDPSSNLSLLISS 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 380 GTHTGAKPHKCPICSKCFTQSSALVTHQRTHTGVKPYPCPECGKCFSQRSNL------------------IAHNRTHTGE 441
Cdd:COG5048   191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSqspsslsssdssssasesPRSSLPTASS 270
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389932 442 -----------------KPYHCLDCGKSFSHSSHLTAHQRTH----RGVRPYSCP--LCGKSFSRRSNLHRHEKIHT 495
Cdd:COG5048   271 qssspnesdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSVnhsgESLKPFSCPysLCGKLFSRNDALKRHILLHT 347
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
309-494 3.19e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 309 CGKRFGRSSHLIQHQIIHTGEKPYTCPSCwKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPH 388
Cdd:COG5048   177 SKDPSSNLSLLISSNVSTSIPSSSENSPL-SSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSS 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 389 KCPICSKCFTQSSALVTHQRTHTGV-------KPYPCPECGKCFSQRSNLIAHNRT--HTGE--KPYHC--LDCGKSFSH 455
Cdd:COG5048   256 SASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSR 335
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720389932 456 SSHLTAHQRTHRGVRPYSCPL--CGKSFSRRSNLHRHEKIH 494
Cdd:COG5048   336 NDALKRHILLHTSISPAKEKLlnSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
398-466 3.37e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 3.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389932 398 TQSSALVTHQRTHTGV----KPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLD--CGKSFSHSSHLTAHQRTH 466
Cdd:COG5048    12 NNSVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
zf-H2C2_2 pfam13465
Zinc-finger double domain;
402-427 3.96e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.96e-05
                          10        20
                  ....*....|....*....|....*.
gi 1720389932 402 ALVTHQRTHTGVKPYPCPECGKCFSQ 427
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
444-466 7.72e-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: 39.59  E-value: 7.72e-05
                          10        20
                  ....*....|....*....|...
gi 1720389932 444 YHCLDCGKSFSHSSHLTAHQRTH 466
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-313 1.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.40e-04
                          10        20
                  ....*....|....*....|....
gi 1720389932 290 HLVTHRRTHTGEKPYTCTDCGKRF 313
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
416-438 2.18e-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: 38.44  E-value: 2.18e-04
                          10        20
                  ....*....|....*....|...
gi 1720389932 416 YPCPECGKCFSQRSNLIAHNRTH 438
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
472-494 2.27e-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: 38.44  E-value: 2.27e-04
                          10        20
                  ....*....|....*....|...
gi 1720389932 472 YSCPLCGKSFSRRSNLHRHEKIH 494
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-455 2.61e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.61e-04
                          10        20
                  ....*....|....*....|....*.
gi 1720389932 430 NLIAHNRTHTGEKPYHCLDCGKSFSH 455
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
388-410 5.99e-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: 37.28  E-value: 5.99e-04
                          10        20
                  ....*....|....*....|...
gi 1720389932 388 HKCPICSKCFTQSSALVTHQRTH 410
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-483 6.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.12e-04
                          10        20
                  ....*....|....*....|....*.
gi 1720389932 458 HLTAHQRTHRGVRPYSCPLCGKSFSR 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
304-326 1.10e-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: 36.51  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|...
gi 1720389932 304 YTCTDCGKRFGRSSHLIQHQIIH 326
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
347-371 1.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*
gi 1720389932 347 LIQHQRIHTGEKPYVCDRCAKRFTR 371
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
328-411 1.24e-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: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 328 GEKPYTCP--SCWKSFSHHSTLIQHqRIHtgekpyvcDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICSKCFTQSSALVT 405
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  ....*.
gi 1720389932 406 HqRTHT 411
Cdd:COG5189   417 H-RKHS 421
PHA00733 PHA00733
hypothetical protein
331-378 1.43e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.70  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720389932 331 PYTCPSCWKSFSHHSTLIQHQRIHTGEKpyVCDRCAKRFTRRSDLVTH 378
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
318-343 1.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|....*.
gi 1720389932 318 HLIQHQIIHTGEKPYTCPSCWKSFSH 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
384-466 1.76e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389932 384 GAKPHKCPI--CSKCFTQSSALVTHQRT-HTGVKPYPCPecgkcfsqrsNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLT 460
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYHMLHgHQNQKLHENP----------SPEKMNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                  ....*.
gi 1720389932 461 AHqRTH 466
Cdd:COG5189   416 YH-RKH 420
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
335-378 2.99e-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: 36.77  E-value: 2.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720389932 335 PSCW---KSFSHHSTLIQHQRIHTgekpYVCDRCAKRFTRRSDLVTH 378
Cdd:cd20908     2 PWCYycdREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-H2C2_2 pfam13465
Zinc-finger double domain;
374-399 3.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.58e-03
                          10        20
                  ....*....|....*....|....*.
gi 1720389932 374 DLVTHQGTHTGAKPHKCPICSKCFTQ 399
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
332-354 4.43e-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: 34.58  E-value: 4.43e-03
                          10        20
                  ....*....|....*....|...
gi 1720389932 332 YTCPSCWKSFSHHSTLIQHQRIH 354
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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