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Conserved domains on  [gi|154759263|ref|NP_776192|]
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zinc finger protein 707 isoform a [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0003677|GO:0008270|GO:0005515|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|8183940|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 1.21e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.54  E-value: 1.21e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154759263     8 VTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALGFCSPRPDLVSRLEQWEEPWV 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
187-366 4.77e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 187 CHSRLLAHQTVHTGTKAF--ECPECGQTFRWASNLQRHQKNHT-------REKPFCCEACGQAFSLKDRLAQHR--KVHT 255
Cdd:COG5048  236 SPKSLLSQSPSSLSSSDSssSASESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLrsVNHS 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 256 --EHRPYSCG--DCGKAFKQKSNLLRHQLVHTGERPFYC--ADCGKAFRTKENLSHHQRVH-----SGEKPYTCAEcGKS 324
Cdd:COG5048  316 geSLKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLS-NSC 394

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 154759263 325 FRWPK---GFSIHRRLHLTKRFYEC--GHCGKGFRHLGFFTRHQRTH 366
Cdd:COG5048  395 IRNFKrdsNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIH 441
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 1.21e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.54  E-value: 1.21e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154759263     8 VTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALGFCSPRPDLVSRLEQWEEPWV 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 2.34e-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: 88.30  E-value: 2.34e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154759263    7 PVTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-47 6.60e-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: 79.13  E-value: 6.60e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 154759263   8 VTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAAL 47
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
187-366 4.77e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 187 CHSRLLAHQTVHTGTKAF--ECPECGQTFRWASNLQRHQKNHT-------REKPFCCEACGQAFSLKDRLAQHR--KVHT 255
Cdd:COG5048  236 SPKSLLSQSPSSLSSSDSssSASESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLrsVNHS 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 256 --EHRPYSCG--DCGKAFKQKSNLLRHQLVHTGERPFYC--ADCGKAFRTKENLSHHQRVH-----SGEKPYTCAEcGKS 324
Cdd:COG5048  316 geSLKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLS-NSC 394

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 154759263 325 FRWPK---GFSIHRRLHLTKRFYEC--GHCGKGFRHLGFFTRHQRTH 366
Cdd:COG5048  395 IRNFKrdsNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIH 441
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 175-324 1.01e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 41.01  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 175 SFICGTCGKALSchSRLLAHQTVHTGTKAFECPE--CGQTFRwasnlQRHQKNHTRekpfcCEACGQAFsLKDRLAQHRK 252
Cdd:PLN03086 407 TVECRNCKHYIP--SRSIALHEAYCSRHNVVCPHdgCGIVLR-----VEEAKNHVH-----CEKCGQAF-QQGEMEKHMK 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 253 VHteHRPYSCGdCGKAFkQKSNLLRHQLVHTGERPFYCADCG-------KAFRTKE---NLSHHQRVhSGEKPYTCAECG 322
Cdd:PLN03086 474 VF--HEPLQCP-CGVVL-EKEQMVQHQASTCPLRLITCRFCGdmvqaggSAMDVRDrlrGMSEHESI-CGSRTAPCDSCG 548


                 ..
gi 154759263 323 KS 324
Cdd:PLN03086 549 RS 550
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 260-282 1.30e-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: 35.74  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|...
gi 154759263  260 YSCGDCGKAFKQKSNLLRHQLVH 282
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 1.21e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.54  E-value: 1.21e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154759263     8 VTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALGFCSPRPDLVSRLEQWEEPWV 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 2.34e-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: 88.30  E-value: 2.34e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154759263    7 PVTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-47 6.60e-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: 79.13  E-value: 6.60e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 154759263   8 VTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAAL 47
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
187-366 4.77e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 187 CHSRLLAHQTVHTGTKAF--ECPECGQTFRWASNLQRHQKNHT-------REKPFCCEACGQAFSLKDRLAQHR--KVHT 255
Cdd:COG5048  236 SPKSLLSQSPSSLSSSDSssSASESPRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLrsVNHS 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 256 --EHRPYSCG--DCGKAFKQKSNLLRHQLVHTGERPFYC--ADCGKAFRTKENLSHHQRVH-----SGEKPYTCAEcGKS 324
Cdd:COG5048  316 geSLKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLS-NSC 394

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 154759263 325 FRWPK---GFSIHRRLHLTKRFYEC--GHCGKGFRHLGFFTRHQRTH 366
Cdd:COG5048  395 IRNFKrdsNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIH 441
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
168-335 7.46e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.09  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 168 KQRAVELSFICGTCGKALSCHSRLLAHQ--TVHTG--TKAFECPE--CGQTFRWASNLQRHQKNHTREKPFCCEAC---- 237
Cdd:COG5048  282 SEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnsss 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 238 --GQAFSLKDRLAQHRKVHTEHRPYSCGD---CGKAFKQKSNLLRHQLVHTGERP--FYCADCGKAFRTKENLSHHQRVH 310
Cdd:COG5048  362 kfSPLLNNEPPQSLQQYKDLKNDKKSETLsnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIH 441

                        170       180
                 ....*....|....*....|....*
gi 154759263 311 SGEKPYTCAECGKSFRWPKGFSIHR 335
Cdd:COG5048  442 TNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-363 4.24e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 4.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 206 CPECGQTFRWASNLQRHQ--KNHTRE--KPFCC--EACGQAFSLKDRLAQHRKVHT--EHRPYSCGDCGKAFKQKSNLLR 277
Cdd:COG5048  292 SKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTsiSPAKEKLLNSSSKFSPLLNNEP 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 278 HQLVH-----TGERPFYCAD--CGKAFRTKENLSHHQRVHSGEKP--YTCAECGKSFRWPKGFSIHRRLHLTKRFYECGH 348
Cdd:COG5048  372 PQSLQqykdlKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSI 451

                        170
                 ....*....|....*
gi 154759263 349 CGKGFRHLGFFTRHQ 363
Cdd:COG5048  452 LKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
204-306 8.21e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 204 FECPECGQTFRWASNLQRHQKNHTREKPFCCEACGQAFSLKDRLAQHRkvHTEHRPYscgdcgkafkQKSNLLRHQLVHT 283
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSR--HLRTHHN----------NPSDLNSKSLPLS 101

                         90       100
                 ....*....|....*....|....*
gi 154759263 284 GERPFYCAD--CGKAFRTKENLSHH 306
Cdd:COG5048  102 NSKASSSSLssSSSNSNDNNLLSSH 126
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 175-324 1.01e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 41.01  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 175 SFICGTCGKALSchSRLLAHQTVHTGTKAFECPE--CGQTFRwasnlQRHQKNHTRekpfcCEACGQAFsLKDRLAQHRK 252
Cdd:PLN03086 407 TVECRNCKHYIP--SRSIALHEAYCSRHNVVCPHdgCGIVLR-----VEEAKNHVH-----CEKCGQAF-QQGEMEKHMK 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154759263 253 VHteHRPYSCGdCGKAFkQKSNLLRHQLVHTGERPFYCADCG-------KAFRTKE---NLSHHQRVhSGEKPYTCAECG 322
Cdd:PLN03086 474 VF--HEPLQCP-CGVVL-EKEQMVQHQASTCPLRLITCRFCGdmvqaggSAMDVRDrlrGMSEHESI-CGSRTAPCDSCG 548


                 ..
gi 154759263 323 KS 324
Cdd:PLN03086 549 RS 550
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 260-282 1.30e-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: 35.74  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|...
gi 154759263  260 YSCGDCGKAFKQKSNLLRHQLVH 282
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
274-299 1.79e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 1.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 154759263  274 NLLRHQLVHTGERPFYCADCGKAFRT 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 ...
 288-310 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: 34.97  E-value: 2.32e-03
                          10        20
                  ....*....|....*....|...
gi 154759263  288 FYCADCGKAFRTKENLSHHQRVH 310
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-325 7.64e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 7.64e-03
                          10        20
                  ....*....|....*....|
gi 154759263  306 HQRVHSGEKPYTCAECGKSF 325
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 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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