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Conserved domains on  [gi|1370475490|ref|XP_024307371|]
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zinc finger protein 302 isoform X1 [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
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-109 2.10e-28

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 106.52  E-value: 2.10e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370475490   48 VTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVSVaGLSVTKPYVIMLLEDGKEPWM 109
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
151-393 7.11e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 7.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 151 SYEFSNSNKNLEYtecdtfrstfhskSTLSEPQNNSAEGNSHKYDILKKNLSKKSVIKSERINGGKKLLNSNKSGAAfNQ 230
Cdd:COG5048   210 SIPSSSSDQNLEN-------------SSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS-SP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 231 SKSLTLPqTCNREKIYTCSECGKAFGKQSILSRHWR--IHTGE--KPYECRE--CGKTFSHGSSLTRHQISHSGEKPYKC 304
Cdd:COG5048   276 NESDSSS-EKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 305 IECGKAFSHGSSLTN-------HQSTHTGEKPYECM--NCGKSFSRVSLLIQHLRIHTQEKRYECR--ICGKAFIHSSSL 373
Cdd:COG5048   355 KLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNL 434

                         250       260
                  ....*....|....*....|
gi 1370475490 374 IHHQKSHTGEKPYECRECGK 393
Cdd:COG5048   435 IPHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
400-425 8.67e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.67e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370475490 400 HLTQHQRIHSMKKKYECNKCLKVFSS 425
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-109 2.10e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 106.52  E-value: 2.10e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370475490   48 VTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVSVaGLSVTKPYVIMLLEDGKEPWM 109
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 48-87 5.36e-21

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: 85.60  E-value: 5.36e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1370475490  48 VTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVSV 87
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 48-86 3.31e-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: 80.29  E-value: 3.31e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370475490  48 VTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVS 86
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
151-393 7.11e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 7.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 151 SYEFSNSNKNLEYtecdtfrstfhskSTLSEPQNNSAEGNSHKYDILKKNLSKKSVIKSERINGGKKLLNSNKSGAAfNQ 230
Cdd:COG5048   210 SIPSSSSDQNLEN-------------SSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS-SP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 231 SKSLTLPqTCNREKIYTCSECGKAFGKQSILSRHWR--IHTGE--KPYECRE--CGKTFSHGSSLTRHQISHSGEKPYKC 304
Cdd:COG5048   276 NESDSSS-EKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 305 IECGKAFSHGSSLTN-------HQSTHTGEKPYECM--NCGKSFSRVSLLIQHLRIHTQEKRYECR--ICGKAFIHSSSL 373
Cdd:COG5048   355 KLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNL 434

                         250       260
                  ....*....|....*....|
gi 1370475490 374 IHHQKSHTGEKPYECRECGK 393
Cdd:COG5048   435 IPHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
288-313 1.09e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.09e-04
                          10        20
                  ....*....|....*....|....*.
gi 1370475490 288 SLTRHQISHSGEKPYKCIECGKAFSH 313
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
400-425 8.67e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.67e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370475490 400 HLTQHQRIHSMKKKYECNKCLKVFSS 425
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
48-109 2.10e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 106.52  E-value: 2.10e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370475490   48 VTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVSVaGLSVTKPYVIMLLEDGKEPWM 109
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 48-87 5.36e-21

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: 85.60  E-value: 5.36e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1370475490  48 VTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVSV 87
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 48-86 3.31e-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: 80.29  E-value: 3.31e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370475490  48 VTFSDVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVS 86
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
151-393 7.11e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 7.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 151 SYEFSNSNKNLEYtecdtfrstfhskSTLSEPQNNSAEGNSHKYDILKKNLSKKSVIKSERINGGKKLLNSNKSGAAfNQ 230
Cdd:COG5048   210 SIPSSSSDQNLEN-------------SSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS-SP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 231 SKSLTLPqTCNREKIYTCSECGKAFGKQSILSRHWR--IHTGE--KPYECRE--CGKTFSHGSSLTRHQISHSGEKPYKC 304
Cdd:COG5048   276 NESDSSS-EKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 305 IECGKAFSHGSSLTN-------HQSTHTGEKPYECM--NCGKSFSRVSLLIQHLRIHTQEKRYECR--ICGKAFIHSSSL 373
Cdd:COG5048   355 KLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNL 434

                         250       260
                  ....*....|....*....|
gi 1370475490 374 IHHQKSHTGEKPYECRECGK 393
Cdd:COG5048   435 IPHKKIHTNHAPLLCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
300-380 2.60e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 300 KPYKCIECGKAFSHGSSLTNHQSTHTGEKPYECM--NCGKSFSRVSLLIQHLRIHTQEKRYECRICGK--AFIHSSSLIH 375
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPlsNSKASSSSLS 111


                  ....*
gi 1370475490 376 HQKSH 380
Cdd:COG5048   112 SSSSN 116
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-442 3.40e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 272 KPYECRECGKTFSHGSSLTRHQ--ISHSGE--KPYKCIE--CGKAFSHGSSLTNHQSTHTGEKPYECMNCGKSFSRVSLL 345
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 346 IQhlrihtqekryecriCGKAFIHSSSLIHHQKSHTGEKPYECRECGKAFCCSSHLTQH--QRIHSMKkkyeCNKCLKVF 423
Cdd:COG5048   368 NN---------------EPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHlsFRPYNCK----NPPCSKSF 428

                         170
                  ....*....|....*....
gi 1370475490 424 SSFSFLVQHQSIHTEEKPF 442
Cdd:COG5048   429 NRHYNLIPHKKIHTNHAPL 447
zf-H2C2_2 pfam13465
Zinc-finger double domain;
288-313 1.09e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.09e-04
                          10        20
                  ....*....|....*....|....*.
gi 1370475490 288 SLTRHQISHSGEKPYKCIECGKAFSH 313
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
261-285 3.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.23e-04
                          10        20
                  ....*....|....*....|....*
gi 1370475490 261 LSRHWRIHTGEKPYECRECGKTFSH 285
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
316-341 8.29e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 8.29e-04
                          10        20
                  ....*....|....*....|....*.
gi 1370475490 316 SLTNHQSTHTGEKPYECMNCGKSFSR 341
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
345-369 1.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....*
gi 1370475490 345 LIQHLRIHTQEKRYECRICGKAFIH 369
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
376-395 1.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.11e-03
                          10        20
                  ....*....|....*....|
gi 1370475490 376 HQKSHTGEKPYECRECGKAF 395
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 358-380 2.99e-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: 2.99e-03
                          10        20
                  ....*....|....*....|...
gi 1370475490 358 YECRICGKAFIHSSSLIHHQKSH 380
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 274-296 8.55e-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: 33.81  E-value: 8.55e-03
                          10        20
                  ....*....|....*....|...
gi 1370475490 274 YECRECGKTFSHGSSLTRHQISH 296
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
400-425 8.67e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.67e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370475490 400 HLTQHQRIHSMKKKYECNKCLKVFSS 425
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 330-352 9.43e-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: 9.43e-03
                          10        20
                  ....*....|....*....|...
gi 1370475490 330 YECMNCGKSFSRVSLLIQHLRIH 352
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
220-434 9.49e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.14  E-value: 9.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 220 NSNKSGAAFNQSKSLTLPQTCNREKIYTCSECGKAFGKQSILSRHWRIHTGEKPYECR--ECGKTFSHGSSLTRHQISHS 297
Cdd:COG5048     8 SSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 298 GEKPYKC-IECGKAFSHGSSLTNHQSTHTGEKPYECMNCGKSFSRVSLLIQHLRIHTQEKRYECRICGKAFIHS--SSLI 374
Cdd:COG5048    88 NNPSDLNsKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475490 375 HHQKSHTgekpyecRECGKAFCCSSHLTQHQRIHSMKKKYECNKCLKvFSSFSFLVQHQS 434
Cdd:COG5048   168 HPPLPAN-------SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQN 219
 
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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