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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 224549028   38 LVTLRDVVINFSQEEWEYLDSAQRNLYWDVMMENYSNLLSLD 79
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224549028 336 KPYKCMHCEKVFRISSQLIEHQRIHTGEKPYAC--KECGKAFGVCRELARHQRIHTGKKPYECKACGKVFRNSSS 408
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAS 106

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 224549028   38 LVTLRDVVINFSQEEWEYLDSAQRNLYWDVMMENYSNLLSLD 79
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 224549028  39 VTLRDVVINFSQEEWEYLDSAQRNLYWDVMMENYSNLLSL 78
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 224549028  408 SLTRHQRIHTGEKPYKCKECEKAF 431
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 294 HAQLTRHQKIHTDEKTYKCMECGKDFRFHSQLTEHQRIHTGEKPYKCMH--CEKVFRISSQLIEHQRIHT 361
Cdd:COG5048   18 STPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHH 87

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 224549028   38 LVTLRDVVINFSQEEWEYLDSAQRNLYWDVMMENYSNLLSLD 79
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 224549028  39 VTLRDVVINFSQEEWEYLDSAQRNLYWDVMMENYSNLLSL 78
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 224549028  408 SLTRHQRIHTGEKPYKCKECEKAF 431
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 300 HQKIHTDEKTYKCMECGkdFRFHSQLTEHQRIHTGeKPYKCMHCEKVFRISSQLIEHQRIH----------TGEKPYACK 369
Cdd:COG5048  217 DQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLS-SSDSSSSASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSK 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 370 ECGKAFgvCRE--LARHQR--IHTGK--KPYECKA--CGKVFRNSSSLTRHQRIHTGEKPYKCK--ECEKAFGVGS---- 435
Cdd:COG5048  294 QCNISF--SRSspLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLnnep 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 436 -ELTRHERIHSGQKPYEC-KECGKFFRLTSALIQHQRIHS---GEKPYECKVCGKAFRHSSALTEHQRIHTGEKPYECKA 510
Cdd:COG5048  372 pQSLQQYKDLKNDKKSETlSNSCIRNFKRDSNLSLHIITHlsfRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSI 451

                 ....*.
gi 224549028 511 CGKAFR 516
Cdd:COG5048  452 LKSFRR 457

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 224549028  492 ALTEHQRIHTGEKPYECKACGKAFRH 517
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 224549028  380 ELARHQRIHTGKKPYECKACGKVFRN 405
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224549028 391 KKPYECKACGKVFRNSSSLTRHQRIHTGEKPYKC--KECEKAFGVGSELTRHERIHSGQKPYEC 452
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLN 94

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 294 HAQLTRHQKIHTDEKTYKCMECGKDFRFHSQLTEHQRIHTGEKPYKCMH--CEKVFRISSQLIEHQRIHT 361
Cdd:COG5048   18 STPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHH 87

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 282 FECSFCGKSFRVHAQLTRHQKIHTDEKTYKCMECGKDFRFH--SQLTEHQRIHTGE------------------------ 335
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNpsdlnskslplsnskasssslsss 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 336 -----KPYKCMHCEKVFRISSQLIEHQRIHTGEKPYACKECGKAFGVCRE----LARHQRIHTGKKPYECKACGKVFRNS 406
Cdd:COG5048  114 ssnsnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQsnslHPPLPANSLSKDPSSNLSLLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 407 SSLTRHQRIHTGEKPYK-------CKECEKAfgvgSELTRHERIHSGQKPY---------------ECKECGKFFRLTSA 464
Cdd:COG5048  194 TSIPSSSENSPLSSSYSipssssdQNLENSS----SSLPLTTNSQLSPKSLlsqspsslsssdsssSASESPRSSLPTAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224549028 465 LIQHQRIHSGE-------KPYECKVCGKAFRHSSALTEHQR--IHTGE--KPYECKA--CGKAFRHSSSFTKHQRIHTDD 531
Cdd:COG5048  270 SQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330
                 ....*....|...
gi 224549028 532 KPYECKECGNSFS 544
Cdd:COG5048  350 SPAKEKLLNSSSK 362

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.

                          10        20
                  ....*....|....*....|...
gi 224549028  394 YECKACGKVFRNSSSLTRHQRIH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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.

                          10        20
                  ....*....|....*....|...
gi 224549028  478 YECKVCGKAFRHSSALTEHQRIH 500
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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.

                          10        20
                  ....*....|....*....|...
gi 224549028  506 YECKACGKAFRHSSSFTKHQRIH 528
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23