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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361395 219 KPYECEECGKVFSHSSNLIKHQRT--HTGE--KPYECD--DCGKTFSQSCSLLEHHKIHTGEKPYQCNM--CGKAFRRNS 290
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361395 291 HLLRHQRIHgdkNVQNPEHGESWESQGrtesqwenteapvsykcNECERSFTRNRSLIEHQKIHTGEKPYQCD--TCGKG 368
Cdd:COG5048   368 NNEPPQSLQ---QYKDLKNDKKSETLS-----------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427

                         170       180
                  ....*....|....*....|.
gi 2217361395 369 FTRTSYLVQHQRSHVGKKTLS 389
Cdd:COG5048   428 FNRHYNLIPHKKIHTNHAPLL 448

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 2217361395 165 HYCHECGKSFAQSSGLTKHRRIH 187
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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 2217361395  66 LKMEDVALTLTP-GWTQLDSSQVNLYRDEKQENHSSLVSL 104
Cdd:cd07765     1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40

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
                  ....*....|....*....|....*....|....*...
gi 2217361395  69 EDVALTLTPG-WTQLDSSQVNLYRDEKQENHSSLVSLG 105
Cdd:pfam01352   5 EDVAVDFTQEeWALLDPAQRNLYRDVMLENYRNLVSLG 42

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 2217361395 180 LTKHRRIHTGEKPYECEDCGKTF 202
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

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 2217361395  66 LKMEDVALTLTP-GWTQLDSSQVNLYRDEKQENHSSLVSL 104
Cdd:cd07765     1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40

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
                  ....*....|....*....|....*....|....*...
gi 2217361395  69 EDVALTLTPG-WTQLDSSQVNLYRDEKQENHSSLVSLG 105
Cdd:pfam01352   5 EDVAVDFTQEeWALLDPAQRNLYRDVMLENYRNLVSLG 42

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 2217361395 235 NLIKHQRTHTGEKPYECDDCGKTFSQ 260
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361395 162 SRRHYCHECGKSFAQSSGLTKHRR--IHTGE--KPYEC--EDCGKTFIGSSALVIHQRVHTGEKPYEC--EECGKVFSHS 233
Cdd:COG5048   287 SLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361395 234 SNLIKHQRTH-----TGEKPYECDD--CGKTFSQSCSLLEHHKIHTGEKPYQCN--MCGKAFRRNSHLLRHQRIHGDKNV 304
Cdd:COG5048   367 LNNEPPQSLQqykdlKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAP 446

                  ....*
gi 2217361395 305 QNPEH 309
Cdd:COG5048   447 LLCSI 451

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 2217361395 277 YQCNMCGKAFRRNSHLLRHQRIH 299
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 2217361395 180 LTKHRRIHTGEKPYECEDCGKTF 202
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361395 165 HYCHECGKSFAQSSGLTKHRRIHTGEKPYECED--CGKTFIGSSALVIHQRVHTGEKPYECE--ECGKVFSHSSNLIKHQ 240
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSksLPLSNSKASSSSLSSS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361395 241 RTHTgEKPYECDDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKAFRRNSHllrHQRIHGDKNVQNpeHGESWESQGRTE 320
Cdd:COG5048   114 SSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQ---SNSLHPPLPANS--LSKDPSSNLSLL 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361395 321 SQWENTEAPVSYKCNECERSFTRNRSLIEHQKIHTGEKPYQCDTCGKGFTRTSYLVQHQ 379
Cdd:COG5048   188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPS 246

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 2217361395 165 HYCHECGKSFAQSSGLTKHRRIH 187
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 2217361395 184 RRIHT-GEKPYECE--DCGKTFIGSSALVIHqRVHTgekpyeceECGKVFSHSSNLIKHQRTHTGEKPYECDDCGKTFsQ 260
Cdd:COG5189   340 RMLKVkDGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-K 409

                          90
                  ....*....|..
gi 2217361395 261 SCSLLEHHKIHT 272
Cdd:COG5189   410 NLNGLKYHRKHS 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 2217361395 360 YQCDTCGKGFTRTSYLVQHQRSH 382
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23