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
                  ....*....|....*....|....*....|....*
gi 1785412827  33 IRCEDVSIYFSLEEWEYIK-GNKALYREGIKEEEE 66
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVMLENYE 35

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1785412827 329 LKEHHRTHTGERPFSCSECGKCFSH 353
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1785412827 413 LTVHRRTHTGEKPFPCPDCGKCFLY 437
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 205 KEEPASSEEDNNFA-DKIQLMD-------NSTVMGRSLDNSTTEHIQGTDTPTPIMGCSLIKSNSNKyDENADISPDKSD 276
Cdd:COG5189   233 YIDIGHMMDTHQFYlEDVDLMDddilgpsNEEMLYKYISPSQGSAELFEESSLGFDYEFIHKSVGNK-EIRGGISTGEMI 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 277 KATNTLCYKYSCNECHKHFTDRRKFDKHQRFH-KREKPFSCS--ECGKSFSYQSQLKeHHRTHtgerpfscsecGKCfSH 353
Cdd:COG5189   312 DVRKLPCTNSSSNGKLAHGGERNIDTPSRMLKvKDGKPYKCPveGCNKKYKNQNGLK-YHMLH-----------GHQ-NQ 378

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1785412827 354 RSHLNSHHRSHTG----EKPFSCSDCGKCFTYQSGLKGHyRTHT 393
Cdd:COG5189   379 KLHENPSPEKMNIfsakDKPYRCEVCDKRYKNLNGLKYH-RKHS 421

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
                  ....*....|....*....|....*....|....*
gi 1785412827  33 IRCEDVSIYFSLEEWEYIK-GNKALYREGIKEEEE 66
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVMLENYE 35

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1785412827 329 LKEHHRTHTGERPFSCSECGKCFSH 353
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1785412827 356 HLNSHHRSHTGEKPFSCSDCGKCFTY 381
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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 1785412827 314 FSCSECGKSFSYQSQLKEHHRTH 336
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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
                  ....*....|....*....|....*....
gi 1785412827  36 EDVSIYFSLEEWEYIK-GNKALYREGIKE 63
Cdd:pfam01352   5 EDVAVDFTQEEWALLDpAQRNLYRDVMLE 33

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 340 RPFSCSECGKCFSHRSHLNSHHRSHTGEKPFSCSDCG---KCFTYQSGLKGHYRTHTGGKSYSCSECGKCFAALSVLTVH 416
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGcdkSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 417 RRTHTGEKPFPCPDCGKCFLYQSHLNNHHRTHTGEKPFYCSECGKCFATSSQRT----------------------VHER 474
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNslhpplpanslskdpssnlsllISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 475 IHTGEKQFPCS*CGKYFGSSSERISHQRRFHTEKPLSCSECgknvFQAHPLLKNISKPRQKRNRFRPWNVVNVILVLNVG 554
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN----SQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1785412827 555 NVFSRHR--NLPSITELTREKPFSCSVCGKGFTRNSNLKIHFQS--HTGE 600
Cdd:COG5048   268 ASSQSSSpnESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGE 317

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
                  ....*....|....*....|....*....|....*
gi 1785412827  33 IRCEDVSIYFSLEEWEYIK-GNKALYREGIKEEEE 66
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVMLENYE 35

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1785412827 329 LKEHHRTHTGERPFSCSECGKCFSH 353
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1785412827 356 HLNSHHRSHTGEKPFSCSDCGKCFTY 381
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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 1785412827 342 FSCSECGKCFSHRSHLNSHHRSH 364
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 205 KEEPASSEEDNNFA-DKIQLMD-------NSTVMGRSLDNSTTEHIQGTDTPTPIMGCSLIKSNSNKyDENADISPDKSD 276
Cdd:COG5189   233 YIDIGHMMDTHQFYlEDVDLMDddilgpsNEEMLYKYISPSQGSAELFEESSLGFDYEFIHKSVGNK-EIRGGISTGEMI 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 277 KATNTLCYKYSCNECHKHFTDRRKFDKHQRFH-KREKPFSCS--ECGKSFSYQSQLKeHHRTHtgerpfscsecGKCfSH 353
Cdd:COG5189   312 DVRKLPCTNSSSNGKLAHGGERNIDTPSRMLKvKDGKPYKCPveGCNKKYKNQNGLK-YHMLH-----------GHQ-NQ 378

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1785412827 354 RSHLNSHHRSHTG----EKPFSCSDCGKCFTYQSGLKGHyRTHT 393
Cdd:COG5189   379 KLHENPSPEKMNIfsakDKPYRCEVCDKRYKNLNGLKYH-RKHS 421

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 1785412827 426 FPCPDCGKCFLYQSHLNNHHRTH 448
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 259 SNSNKYDENADISPDKSDKATNTLCYKYSCNECHKHFTDRRKFDKHQRFHKREKPFSCS--ECGKSFSYQSQLKEHHRTH 336
Cdd:COG5048     7 QSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 337 TGERPFSCS-ECGKCFSHRSHLNSHHRSHTGEKPFSCSDCGKCFTYQSGLKGHYRTHTGGKSYSCSEC----GKCFAALS 411
Cdd:COG5048    87 HNNPSDLNSkSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnsssVNTPQSNS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 412 VLTVHRRTHTGEKPFPCPDCGKC----FLYQSHLNNHHRTHTGEKPFYCSECGKCFATSSQrTVHERIHTGEKQFPCS*c 487
Cdd:COG5048   167 LHPPLPANSLSKDPSSNLSLLISsnvsTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL-PLTTNSQLSPKSLLSQ-- 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785412827 488 gkyfgSSSERISHQRRFHTEKPLSCSECGKNVFQAHPLLKNISKPRQKRNRFRpwnVVNVILVLNVGNVFSRHRNLpSIT 567
Cdd:COG5048   244 -----SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIK---SKQCNISFSRSSPLTRHLRS-VNH 314

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1785412827 568 ELTREKPFSC--SVCGKGFTRNSNLKIHFQSHTG 599
Cdd:COG5048   315 SGESLKPFSCpySLCGKLFSRNDALKRHILLHTS 348

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 1785412827 575 FSCSVCGKGFTRNSNLKIHFQSH 597
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23