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Conserved domains on  [gi|1371542794|ref|NP_001348394|]
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zinc finger protein 707 isoform 4 [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204351)

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

Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  22803940|14519192|8183940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
26-86 2.72e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.37  E-value: 2.72e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371542794   26 VTFRDVAVYFCREEWECLSPSQRTLYRNVMLENFRNLNELGCCSRRPGLITRLEQWDEPWV 86
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
156-335 2.82e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 156 SHRKQPDLKEQGQSGPEGQPFICGICGKALSCHSRLAAHQ--TVHTG--TRSFECLE--CGRTFRWASNLLRHQRNHTSE 229
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 230 KPFCCELC------GQAFSLKDRL-AQHRKIHTEHRPYEC--GDCGKAFKQKSNLLRHKLVHTGEKP--FYCDTCGKAFR 298
Cdd:COG5048   350 SPAKEKLLnssskfSPLLNNEPPQsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFN 429

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371542794 299 TKENLSHHQRIHSGEKPYTCGECGKAFRWPKGFSIHQ 335
Cdd:COG5048   430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 344-366 9.00e-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: 33.43  E-value: 9.00e-03
                          10        20
                  ....*....|....*....|...
gi 1371542794 344 YQCEQCGKGFRHLGFFTRHQRTH 366
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
26-86 2.72e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.37  E-value: 2.72e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371542794   26 VTFRDVAVYFCREEWECLSPSQRTLYRNVMLENFRNLNELGCCSRRPGLITRLEQWDEPWV 86
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 25-66 1.48e-22

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: 89.07  E-value: 1.48e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1371542794  25 PVTFRDVAVYFCREEWECLSPSQRTLYRNVMLENFRNLNELG 66
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 26-62 4.78e-19

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: 79.52  E-value: 4.78e-19
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1371542794  26 VTFRDVAVYFCREEWECLSPSQRTLYRNVMLENFRNL 62
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENL 37
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
156-335 2.82e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 156 SHRKQPDLKEQGQSGPEGQPFICGICGKALSCHSRLAAHQ--TVHTG--TRSFECLE--CGRTFRWASNLLRHQRNHTSE 229
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 230 KPFCCELC------GQAFSLKDRL-AQHRKIHTEHRPYEC--GDCGKAFKQKSNLLRHKLVHTGEKP--FYCDTCGKAFR 298
Cdd:COG5048   350 SPAKEKLLnssskfSPLLNNEPPQsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFN 429

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371542794 299 TKENLSHHQRIHSGEKPYTCGECGKAFRWPKGFSIHQ 335
Cdd:COG5048   430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
274-299 2.48e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 2.48e-04
                          10        20
                  ....*....|....*....|....*.
gi 1371542794 274 NLLRHKLVHTGEKPFYCDTCGKAFRT 299
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 344-366 9.00e-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: 33.43  E-value: 9.00e-03
                          10        20
                  ....*....|....*....|...
gi 1371542794 344 YQCEQCGKGFRHLGFFTRHQRTH 366
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
26-86 2.72e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.37  E-value: 2.72e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371542794   26 VTFRDVAVYFCREEWECLSPSQRTLYRNVMLENFRNLNELGCCSRRPGLITRLEQWDEPWV 86
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 25-66 1.48e-22

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: 89.07  E-value: 1.48e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1371542794  25 PVTFRDVAVYFCREEWECLSPSQRTLYRNVMLENFRNLNELG 66
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 26-62 4.78e-19

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: 79.52  E-value: 4.78e-19
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1371542794  26 VTFRDVAVYFCREEWECLSPSQRTLYRNVMLENFRNL 62
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENL 37
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
156-335 2.82e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 156 SHRKQPDLKEQGQSGPEGQPFICGICGKALSCHSRLAAHQ--TVHTG--TRSFECLE--CGRTFRWASNLLRHQRNHTSE 229
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 230 KPFCCELC------GQAFSLKDRL-AQHRKIHTEHRPYEC--GDCGKAFKQKSNLLRHKLVHTGEKP--FYCDTCGKAFR 298
Cdd:COG5048   350 SPAKEKLLnssskfSPLLNNEPPQsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFN 429

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371542794 299 TKENLSHHQRIHSGEKPYTCGECGKAFRWPKGFSIHQ 335
Cdd:COG5048   430 RHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
201-363 2.92e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.17  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 201 TRSFECLECGRTFRWASNLLRHQR--NHTSE--KPFCC--ELCGQAFSLKDRLAQHRKIHTEHRPYEC--GDCGKAFKQK 272
Cdd:COG5048   287 SLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 273 SNLLRHKLVH-----TGEKPFYCD--TCGKAFRTKENLSHH--QRIHSGEKPYTCGECGKAFRWPKGFSIHQRLHLTKKF 343
Cdd:COG5048   367 LNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAP 446

                         170       180
                  ....*....|....*....|
gi 1371542794 344 YQCEQCGKGFRHLGFFTRHQ 363
Cdd:COG5048   447 LLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
178-366 6.11e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 178 CGICGKALSCHSRLAAHQTVHTGTRSFECLECGRTFRWASNLLRHQRNHTSE-------KPFCCELCGQAFSLKDRLAQH 250
Cdd:COG5048   229 LTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRH 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 251 R--KIHT--EHRPYECG--DCGKAFKQKSNLLRHKLVHTGEKPFYC--DTCGKAFRTKENLSHHQRIH-----SGEKPYT 317
Cdd:COG5048   309 LrsVNHSgeSLKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSE 388

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371542794 318 C--GECGKAFRWPKGFSIHQRLHLTKKFYQCE--QCGKGFRHLGFFTRHQRTH 366
Cdd:COG5048   389 TlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
201-306 9.35e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 9.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371542794 201 TRSFECLECGRTFRWASNLLRHQRNHTSEKPFCCELCGQAFSLKDRLAQHRkiHTEHRPYecgdcgkafkQKSNLLRHKL 280
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSR--HLRTHHN----------NPSDLNSKSL 98

                          90       100
                  ....*....|....*....|....*...
gi 1371542794 281 VHTGEKPFYC--DTCGKAFRTKENLSHH 306
Cdd:COG5048    99 PLSNSKASSSslSSSSSNSNDNNLLSSH 126
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
258-318 4.33e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 4.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371542794 258 RPYECGDCGKAFKQKSNLLRHKLVHTGEKPFYC--DTCGKAFRTKENLSHHQRIHSGEKPYTC 318
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLN 94
zf-H2C2_2 pfam13465
Zinc-finger double domain;
274-299 2.48e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 2.48e-04
                          10        20
                  ....*....|....*....|....*.
gi 1371542794 274 NLLRHKLVHTGEKPFYCDTCGKAFRT 299
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
286-338 4.07e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 4.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371542794 286 KPFYCDTCGKAFRTKENLSHHQRIHSGEKPYTCG--ECGKAFRWPKGFSIHQRLH 338
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 288-310 2.07e-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: 2.07e-03
                          10        20
                  ....*....|....*....|...
gi 1371542794 288 FYCDTCGKAFRTKENLSHHQRIH 310
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 260-282 2.17e-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: 34.97  E-value: 2.17e-03
                          10        20
                  ....*....|....*....|...
gi 1371542794 260 YECGDCGKAFKQKSNLLRHKLVH 282
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
246-271 3.73e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 3.73e-03
                          10        20
                  ....*....|....*....|....*.
gi 1371542794 246 RLAQHRKIHTEHRPYECGDCGKAFKQ 271
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-325 4.72e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 4.72e-03
                          10        20
                  ....*....|....*....|
gi 1371542794 306 HQRIHSGEKPYTCGECGKAF 325
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 344-366 9.00e-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: 33.43  E-value: 9.00e-03
                          10        20
                  ....*....|....*....|...
gi 1371542794 344 YQCEQCGKGFRHLGFFTRHQRTH 366
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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