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Conserved domains on  [gi|55769570|ref|NP_116214|]
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zinc finger protein 382 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204794)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-67 4.93e-36

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 128.48  E-value: 4.93e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55769570      7 VSFKDVTVDFTQEEWQQLDPAQKALYRDVMLENYCHFVSVGFHMAKPDMIRKLEQGEELWT 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
354-533 5.56e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 5.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 354 CIDCGKSFRQKATLTRHHKTHTGE-------KAYECPQCGSAFRKKSYLIDHQRT--HTGE--KPYQCNE--CGKAFIQK 420
Cdd:COG5048 257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 421 TTLTVHQRTHTGEKPYIC--NECGKSFCQKTTLTLHQRI--HTGEKPYICNECGKSFRQKAILTVH----HRIHTGEKSN 492
Cdd:COG5048 337 DALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLqqYKDLKNDKKSETLSNSCIRNFKRDSnlslHIITHLSFRP 416

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 55769570 493 G---CPQCGKAFSRKSNLIRHQKTHTGEKPYECKQCGKFFSCKS 533
Cdd:COG5048 417 YnckNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
310-335 3.50e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.50e-04
                          10        20
                  ....*....|....*....|....*.
gi 55769570   310 YLIEHQRIHTGEKPYVCNQCGKAFRQ 335
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-67 4.93e-36

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 128.48  E-value: 4.93e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55769570      7 VSFKDVTVDFTQEEWQQLDPAQKALYRDVMLENYCHFVSVGFHMAKPDMIRKLEQGEELWT 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 6-47 6.26e-24

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: 94.07  E-value: 6.26e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 55769570     6 SVSFKDVTVDFTQEEWQQLDPAQKALYRDVMLENYCHFVSVG 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 7-45 6.40e-20

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: 82.98  E-value: 6.40e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 55769570   7 VSFKDVTVDFTQEEWQQLDPAQKALYRDVMLENYCHFVS 45
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
354-533 5.56e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 5.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 354 CIDCGKSFRQKATLTRHHKTHTGE-------KAYECPQCGSAFRKKSYLIDHQRT--HTGE--KPYQCNE--CGKAFIQK 420
Cdd:COG5048 257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 421 TTLTVHQRTHTGEKPYIC--NECGKSFCQKTTLTLHQRI--HTGEKPYICNECGKSFRQKAILTVH----HRIHTGEKSN 492
Cdd:COG5048 337 DALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLqqYKDLKNDKKSETLSNSCIRNFKRDSnlslHIITHLSFRP 416

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 55769570 493 G---CPQCGKAFSRKSNLIRHQKTHTGEKPYECKQCGKFFSCKS 533
Cdd:COG5048 417 YnckNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
506-531 5.44e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.44e-05
                          10        20
                  ....*....|....*....|....*.
gi 55769570   506 NLIRHQKTHTGEKPYECKQCGKFFSC 531
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
310-335 3.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.50e-04
                          10        20
                  ....*....|....*....|....*.
gi 55769570   310 YLIEHQRIHTGEKPYVCNQCGKAFRQ 335
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-67 4.93e-36

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 128.48  E-value: 4.93e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55769570      7 VSFKDVTVDFTQEEWQQLDPAQKALYRDVMLENYCHFVSVGFHMAKPDMIRKLEQGEELWT 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 6-47 6.26e-24

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: 94.07  E-value: 6.26e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 55769570     6 SVSFKDVTVDFTQEEWQQLDPAQKALYRDVMLENYCHFVSVG 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 7-45 6.40e-20

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: 82.98  E-value: 6.40e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 55769570   7 VSFKDVTVDFTQEEWQQLDPAQKALYRDVMLENYCHFVS 45
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
354-533 5.56e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 5.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 354 CIDCGKSFRQKATLTRHHKTHTGE-------KAYECPQCGSAFRKKSYLIDHQRT--HTGE--KPYQCNE--CGKAFIQK 420
Cdd:COG5048 257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRN 336

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 421 TTLTVHQRTHTGEKPYIC--NECGKSFCQKTTLTLHQRI--HTGEKPYICNECGKSFRQKAILTVH----HRIHTGEKSN 492
Cdd:COG5048 337 DALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLqqYKDLKNDKKSETLSNSCIRNFKRDSnlslHIITHLSFRP 416

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 55769570 493 G---CPQCGKAFSRKSNLIRHQKTHTGEKPYECKQCGKFFSCKS 533
Cdd:COG5048 417 YnckNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
288-523 8.86e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 8.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 288 RPQTEEKPFHCPY--CGNNFRRKSYLIEHQRIHTGEKPYVCNQ----------------CGKAFRQKTALTLHEKTHIEG 349
Cdd:COG5048  54 RSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKslplsnskasssslssSSSNSNDNNLLSSHSLPPSSR 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 350 KPFICIDCGKSFRQKATLTR-----------------------------------HHKTHTGEKAYECPQCGSAFRKKSY 394
Cdd:COG5048 134 DPQLPDLLSISNLRNNPLPGnnsssvntpqsnslhpplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPS 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 395 LIDHQRTHTGEKPYQCNECGKAF------IQKTTLTVHQRTHTGEKPYICNECGKSFCQKTTLTLHQRIHTG-EKPYICN 467
Cdd:COG5048 214 SSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSK 293

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55769570 468 ECGKSFRQKAILTVH--HRIHTGEKSNG--CP--QCGKAFSRKSNLIRHQKTHTGEKPYECK 523
Cdd:COG5048 294 QCNISFSRSSPLTRHlrSVNHSGESLKPfsCPysLCGKLFSRNDALKRHILLHTSISPAKEK 355
zf-H2C2_2 pfam13465
Zinc-finger double domain;
506-531 5.44e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.44e-05
                          10        20
                  ....*....|....*....|....*.
gi 55769570   506 NLIRHQKTHTGEKPYECKQCGKFFSC 531
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
394-419 2.02e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.02e-04
                          10        20
                  ....*....|....*....|....*.
gi 55769570   394 YLIDHQRTHTGEKPYQCNECGKAFIQ 419
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
310-335 3.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.50e-04
                          10        20
                  ....*....|....*....|....*.
gi 55769570   310 YLIEHQRIHTGEKPYVCNQCGKAFRQ 335
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
294-422 4.30e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 4.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55769570 294 KPFHCPY--CGNNFRRKSYLIEHQRIHTGEKPYVC--NQCGKAFRQK-----TALTLHEKTHIEGKPFICID--CGKSFR 362
Cdd:COG5048 320 KPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLSnsCIRNFK 399

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55769570 363 QKATLTRHHKTHT--GEKAYECPQCGSAFRKKSYLIDHQRTHTGEKPYQCNECGKAFIQKTT 422
Cdd:COG5048 400 RDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
490-542 5.77e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 5.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55769570 490 KSNGCPQCGKAFSRKSNLIRHQKTHTGEKPYECKQCGKFFSCK--SNLIVHQKTH 542
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 494-514 9.89e-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: 36.51  E-value: 9.89e-04
                          10        20
                  ....*....|....*....|.
gi 55769570   494 CPQCGKAFSRKSNLIRHQKTH 514
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 408-430 2.32e-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: 35.35  E-value: 2.32e-03
                          10        20
                  ....*....|....*....|...
gi 55769570   408 YQCNECGKAFIQKTTLTVHQRTH 430
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-389 4.20e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.20e-03
                          10        20
                  ....*....|....*....|...
gi 55769570   367 LTRHHKTHTGEKAYECPQCGSAF 389
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 436-458 5.78e-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: 5.78e-03
                          10        20
                  ....*....|....*....|...
gi 55769570   436 YICNECGKSFCQKTTLTLHQRIH 458
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
451-475 7.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.14e-03
                          10        20
                  ....*....|....*....|....*
gi 55769570   451 LTLHQRIHTGEKPYICNECGKSFRQ 475
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
423-445 8.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.96e-03
                          10        20
                  ....*....|....*....|...
gi 55769570   423 LTVHQRTHTGEKPYICNECGKSF 445
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
 
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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