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Conserved domains on  [gi|564372734|ref|XP_006246757|]
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zinc finger protein 18 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
37-144 2.53e-50

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 168.64  E-value: 2.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734    37 PETARQLFRQFRYQVMSGPQETLRQLRKLCFQWLRPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLV 116
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|....*...
gi 564372734   117 ESLKGDPQKLWQWISIQVLGQEIPFEKE 144
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKM 108
KRAB super family cl42959
krueppel associated box;
229-278 4.03e-08

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 49.90  E-value: 4.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564372734   229 EEQWRHLDSTQKEQYWDLMLETYGKMVSgvAGISNSKPDLTNMAEYGEEL 278
Cdd:smart00349  12 QEEWEQLDPAQKNLYRDVMLENYSNLVS--LGFQVPKPDLISQLEQGEEP 59
zf-H2C2_2 pfam13465
Zinc-finger double domain;
513-537 1.42e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.42e-06
                          10        20
                  ....*....|....*....|....*
gi 564372734  513 NFNRHQRVHTGEKPYKCTHCGKRFS 537
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
428-521 3.12e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734 428 SQLVFHQRTHTGETYFH-CRICKKAFLRSSDFVKHQRT--HTGE--KPCKCDY--CGKGFSDFSGLRHHEKIHTGEKPYK 500
Cdd:COG5048  274 SPNESDSSSEKGFSLPIkSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                         90       100
                 ....*....|....*....|...
gi 564372734 501 CPI--CEKSFIQRSNFNRHQRVH 521
Cdd:COG5048  354 EKLlnSSSKFSPLLNNEPPQSLQ 376
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 527-549 1.28e-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: 1.28e-03
                          10        20
                  ....*....|....*....|...
gi 564372734  527 YKCTHCGKRFSWSSSLDKHQRSH 549
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
37-144 2.53e-50

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 168.64  E-value: 2.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734    37 PETARQLFRQFRYQVMSGPQETLRQLRKLCFQWLRPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLV 116
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|....*...
gi 564372734   117 ESLKGDPQKLWQWISIQVLGQEIPFEKE 144
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKM 108
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 37-125 1.18e-44

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 152.64  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734   37 PETARQLFRQFRYQVMSGPQETLRQLRKLCFQWLRPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLV 116
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 564372734  117 ESLKGDPQK 125
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 37-120 7.41e-37

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 131.61  E-value: 7.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734  37 PETARQLFRQFRYQVMSGPQETLRQLRKLCFQWLRPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLV 116
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....
gi 564372734 117 ESLK 120
Cdd:cd07936   81 EDLL 84
KRAB smart00349
krueppel associated box;
229-278 4.03e-08

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 49.90  E-value: 4.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564372734   229 EEQWRHLDSTQKEQYWDLMLETYGKMVSgvAGISNSKPDLTNMAEYGEEL 278
Cdd:smart00349  12 QEEWEQLDPAQKNLYRDVMLENYSNLVS--LGFQVPKPDLISQLEQGEEP 59
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 226-256 1.09e-07

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: 47.93  E-value: 1.09e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 564372734 226 SLQEEQWRHLDSTQKEQYWDLMLETYGKMVS 256
Cdd:cd07765    9 YFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 229-256 9.17e-07

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: 45.54  E-value: 9.17e-07
                          10        20
                  ....*....|....*....|....*...
gi 564372734  229 EEQWRHLDSTQKEQYWDLMLETYGKMVS 256
Cdd:pfam01352  13 QEEWALLDPAQRNLYRDVMLENYRNLVS 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
513-537 1.42e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.42e-06
                          10        20
                  ....*....|....*....|....*
gi 564372734  513 NFNRHQRVHTGEKPYKCTHCGKRFS 537
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
428-521 3.12e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734 428 SQLVFHQRTHTGETYFH-CRICKKAFLRSSDFVKHQRT--HTGE--KPCKCDY--CGKGFSDFSGLRHHEKIHTGEKPYK 500
Cdd:COG5048  274 SPNESDSSSEKGFSLPIkSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                         90       100
                 ....*....|....*....|...
gi 564372734 501 CPI--CEKSFIQRSNFNRHQRVH 521
Cdd:COG5048  354 EKLlnSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
497-549 6.14e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 6.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564372734 497 KPYKCPICEKSFIQRSNFNRHQRVHTGEKPYKCTH--CGKRFSWSSSLDKHQRSH 549
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 499-521 9.80e-06

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: 42.29  E-value: 9.80e-06
                          10        20
                  ....*....|....*....|...
gi 564372734  499 YKCPICEKSFIQRSNFNRHQRVH 521
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 527-549 1.28e-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: 1.28e-03
                          10        20
                  ....*....|....*....|...
gi 564372734  527 YKCTHCGKRFSWSSSLDKHQRSH 549
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
499-521 1.41e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 1.41e-03
                           10        20
                   ....*....|....*....|...
gi 564372734   499 YKCPICEKSFIQRSNFNRHQRVH 521
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
527-549 2.84e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.84e-03
                           10        20
                   ....*....|....*....|...
gi 564372734   527 YKCTHCGKRFSWSSSLDKHQRSH 549
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
37-144 2.53e-50

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 168.64  E-value: 2.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734    37 PETARQLFRQFRYQVMSGPQETLRQLRKLCFQWLRPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLV 116
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100
                   ....*....|....*....|....*...
gi 564372734   117 ESLKGDPQKLWQWISIQVLGQEIPFEKE 144
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKM 108
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 37-125 1.18e-44

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 152.64  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734   37 PETARQLFRQFRYQVMSGPQETLRQLRKLCFQWLRPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLV 116
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 564372734  117 ESLKGDPQK 125
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 37-120 7.41e-37

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 131.61  E-value: 7.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734  37 PETARQLFRQFRYQVMSGPQETLRQLRKLCFQWLRPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLV 116
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....
gi 564372734 117 ESLK 120
Cdd:cd07936   81 EDLL 84
KRAB smart00349
krueppel associated box;
229-278 4.03e-08

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 49.90  E-value: 4.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564372734   229 EEQWRHLDSTQKEQYWDLMLETYGKMVSgvAGISNSKPDLTNMAEYGEEL 278
Cdd:smart00349  12 QEEWEQLDPAQKNLYRDVMLENYSNLVS--LGFQVPKPDLISQLEQGEEP 59
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 226-256 1.09e-07

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: 47.93  E-value: 1.09e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 564372734 226 SLQEEQWRHLDSTQKEQYWDLMLETYGKMVS 256
Cdd:cd07765    9 YFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 229-256 9.17e-07

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: 45.54  E-value: 9.17e-07
                          10        20
                  ....*....|....*....|....*...
gi 564372734  229 EEQWRHLDSTQKEQYWDLMLETYGKMVS 256
Cdd:pfam01352  13 QEEWALLDPAQRNLYRDVMLENYRNLVS 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
513-537 1.42e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 1.42e-06
                          10        20
                  ....*....|....*....|....*
gi 564372734  513 NFNRHQRVHTGEKPYKCTHCGKRFS 537
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
428-521 3.12e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.69  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734 428 SQLVFHQRTHTGETYFH-CRICKKAFLRSSDFVKHQRT--HTGE--KPCKCDY--CGKGFSDFSGLRHHEKIHTGEKPYK 500
Cdd:COG5048  274 SPNESDSSSEKGFSLPIkSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                         90       100
                 ....*....|....*....|...
gi 564372734 501 CPI--CEKSFIQRSNFNRHQRVH 521
Cdd:COG5048  354 EKLlnSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
497-549 6.14e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 6.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564372734 497 KPYKCPICEKSFIQRSNFNRHQRVHTGEKPYKCTH--CGKRFSWSSSLDKHQRSH 549
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 499-521 9.80e-06

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: 42.29  E-value: 9.80e-06
                          10        20
                  ....*....|....*....|...
gi 564372734  499 YKCPICEKSFIQRSNFNRHQRVH 521
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
489-510 9.98e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 9.98e-06
                          10        20
                  ....*....|....*....|..
gi 564372734  489 HEKIHTGEKPYKCPICEKSFIQ 510
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
433-556 1.30e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734 433 HQRTHTGETYFHCRIcKKAFLRSSDFVKHQRTHTG-EKPCKCDYCGKGFSDFSGLRHH--EKIHTGE--KPYKCPI--CE 505
Cdd:COG5048  252 DSSSSASESPRSSLP-TASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCG 330

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564372734 506 KSFIQRSNFNRHQRVHTGEKPYKC--THCGKRFSWSSSLDKHQRSHLGKKPCP 556
Cdd:COG5048  331 KLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQYKDLKN 383
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 455-549 2.22e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734 455 SSDFVKHQRTHTGEKPCKCDYCGKGFS-------DFSGLRHHEKihtGEKPYKCPI--CEKSFiQRSNFNRHQRVH---- 521
Cdd:COG5189  302 RGGISTGEMIDVRKLPCTNSSSNGKLAhggerniDTPSRMLKVK---DGKPYKCPVegCNKKY-KNQNGLKYHMLHghqn 377

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564372734 522 ----------------TGEKPYKCTHCGKRFSWSSSLdKHQRSH 549
Cdd:COG5189  378 qklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGL-KYHRKH 420
zf-H2C2_2 pfam13465
Zinc-finger double domain;
460-481 1.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.11e-03
                          10        20
                  ....*....|....*....|..
gi 564372734  460 KHQRTHTGEKPCKCDYCGKGFS 481
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 527-549 1.28e-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: 1.28e-03
                          10        20
                  ....*....|....*....|...
gi 564372734  527 YKCTHCGKRFSWSSSLDKHQRSH 549
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
441-517 1.35e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564372734 441 TYFHCRICKKAFLRSSDFVKHQRTHTGEKPCKCDY--CGKGFSDFSGLRHHEKIHTGEKPYKcpiCEKSFIQRSNFNRH 517
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDL---NSKSLPLSNSKASS 107
ZnF_C2H2 smart00355
zinc finger;
499-521 1.41e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 1.41e-03
                           10        20
                   ....*....|....*....|...
gi 564372734   499 YKCPICEKSFIQRSNFNRHQRVH 521
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-Di19 pfam05605
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ...
 472-506 1.79e-03

Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain.


Pssm-ID: 428539  Cd Length: 54  Bit Score: 36.51  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564372734  472 KCDYCGKGFSDFSGLRHHEKIHTGE-KPYKCPICEK 506
Cdd:pfam05605   4 TCPFCGEDFDVVSLCEHVEDEHPVEsKNVVCPVCAA 39
ZnF_C2H2 smart00355
zinc finger;
527-549 2.84e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.84e-03
                           10        20
                   ....*....|....*....|...
gi 564372734   527 YKCTHCGKRFSWSSSLDKHQRSH 549
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 443-465 5.46e-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: 5.46e-03
                          10        20
                  ....*....|....*....|...
gi 564372734  443 FHCRICKKAFLRSSDFVKHQRTH 465
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
417-507 9.45e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 9.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372734 417 CRECGKTFYRNSQLVFHQRTHTGETYFHCR--ICKKAFLRSSDFVKHQRTHTGEKPCKCDYCGKgfSDFSGLRHHEKIHT 494
Cdd:COG5048   36 CPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP--LSNSKASSSSLSSS 113

                         90
                 ....*....|...
gi 564372734 495 GEKPYKCPICEKS 507
Cdd:COG5048  114 SSNSNDNNLLSSH 126
 
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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