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Conserved domains on  [gi|1622897150|ref|XP_014979013|]
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zinc finger protein 302 isoform X3 [Macaca mulatta]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-65 3.03e-28

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.37  E-value: 3.03e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897150    4 VTFSDVAIDFSHEEWAWLDSAQRDLYKDVMVQNYENLVSVaGLSITKPYVIMLLEDGKEPWM 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL-GFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
228-398 1.54e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 228 KPYECRECGKTFSHGSSLTRHQ--ISHSGE--KPYKCVE--CGKAFSHGSSLTNHQSTHTGEKPYECMNCGKSFSRVSLL 301
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 302 IQhlrihtqekryecriCGKAFIHSSSLIHHQKSHTGEKPYECRECGKAFCCSSHLTQHqgIHSIKKKFECNKCLKVFSS 381
Cdd:COG5048   368 NN---------------EPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITH--LSFRPYNCKNPPCSKSFNR 430
                         170
                  ....*....|....*..
gi 1622897150 382 LSFLVQHQSIHTEENPF 398
Cdd:COG5048   431 HYNLIPHKKIHTNHAPL 447
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-65 3.03e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.37  E-value: 3.03e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897150    4 VTFSDVAIDFSHEEWAWLDSAQRDLYKDVMVQNYENLVSVaGLSITKPYVIMLLEDGKEPWM 65
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 ...
4-43 2.00e-20

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: 83.67  E-value: 2.00e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622897150   4 VTFSDVAIDFSHEEWAWLDSAQRDLYKDVMVQNYENLVSV 43
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
4-42 6.27e-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: 6.27e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622897150   4 VTFSDVAIDFSHEEWAWLDSAQRDLYKDVMVQNYENLVS 42
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
228-398 1.54e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 228 KPYECRECGKTFSHGSSLTRHQ--ISHSGE--KPYKCVE--CGKAFSHGSSLTNHQSTHTGEKPYECMNCGKSFSRVSLL 301
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 302 IQhlrihtqekryecriCGKAFIHSSSLIHHQKSHTGEKPYECRECGKAFCCSSHLTQHqgIHSIKKKFECNKCLKVFSS 381
Cdd:COG5048   368 NN---------------EPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITH--LSFRPYNCKNPPCSKSFNR 430
                         170
                  ....*....|....*..
gi 1622897150 382 LSFLVQHQSIHTEENPF 398
Cdd:COG5048   431 HYNLIPHKKIHTNHAPL 447
zf-H2C2_2 pfam13465
Zinc-finger double domain;
217-241 1.91e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.91e-04
                          10        20
                  ....*....|....*....|....*
gi 1622897150 217 LNRHWRIHTGEKPYECRECGKTFSH 241
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
285-332 9.61e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.01  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622897150 285 PYECMNCGKSFSRVSLLIQHLRIHTQEKRyeCRICGKAFIHSSSLIHH 332
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSKV--CPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-65 3.03e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.37  E-value: 3.03e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897150    4 VTFSDVAIDFSHEEWAWLDSAQRDLYKDVMVQNYENLVSVaGLSITKPYVIMLLEDGKEPWM 65
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 ...
4-43 2.00e-20

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: 83.67  E-value: 2.00e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622897150   4 VTFSDVAIDFSHEEWAWLDSAQRDLYKDVMVQNYENLVSV 43
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
4-42 6.27e-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: 6.27e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622897150   4 VTFSDVAIDFSHEEWAWLDSAQRDLYKDVMVQNYENLVS 42
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
228-398 1.54e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 228 KPYECRECGKTFSHGSSLTRHQ--ISHSGE--KPYKCVE--CGKAFSHGSSLTNHQSTHTGEKPYECMNCGKSFSRVSLL 301
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 302 IQhlrihtqekryecriCGKAFIHSSSLIHHQKSHTGEKPYECRECGKAFCCSSHLTQHqgIHSIKKKFECNKCLKVFSS 381
Cdd:COG5048   368 NN---------------EPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITH--LSFRPYNCKNPPCSKSFNR 430
                         170
                  ....*....|....*..
gi 1622897150 382 LSFLVQHQSIHTEENPF 398
Cdd:COG5048   431 HYNLIPHKKIHTNHAPL 447
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
200-349 5.38e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 200 KIYTCSECGKAFGKQSILNRHWR--IHTGE--KPYECRE--CGKTFSHGSSLTRHQISHSGEKPYKCVECGKAFSHGSSL 273
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 274 TN-------HQSTHTGEKPYECM--NCGKSFSRVSLLIQHLRIHTQEKRYECR--ICGKAFIHSSSLIHHQKSHTGEKPY 342
Cdd:COG5048   368 NNeppqslqQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL 447

                  ....*..
gi 1622897150 343 ECRECGK 349
Cdd:COG5048   448 LCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
256-336 6.64e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897150 256 KPYKCVECGKAFSHGSSLTNHQSTHTGEKPYECM--NCGKSFSRVSLLIQHLRIHTQEKRYECRICGK--AFIHSSSLIH 331
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPlsNSKASSSSLS 111

                  ....*
gi 1622897150 332 HQKSH 336
Cdd:COG5048   112 SSSSN 116
zf-H2C2_2 pfam13465
Zinc-finger double domain;
217-241 1.91e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.91e-04
                          10        20
                  ....*....|....*....|....*
gi 1622897150 217 LNRHWRIHTGEKPYECRECGKTFSH 241
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
272-297 6.92e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 6.92e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622897150 272 SLTNHQSTHTGEKPYECMNCGKSFSR 297
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
301-325 8.68e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 8.68e-04
                          10        20
                  ....*....|....*....|....*
gi 1622897150 301 LIQHLRIHTQEKRYECRICGKAFIH 325
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
332-351 9.29e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 9.29e-04
                          10        20
                  ....*....|....*....|
gi 1622897150 332 HQKSHTGEKPYECRECGKAF 351
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
244-269 1.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622897150 244 SLTRHQISHSGEKPYKCVECGKAFSH 269
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
314-336 2.70e-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: 2.70e-03
                          10        20
                  ....*....|....*....|...
gi 1622897150 314 YECRICGKAFIHSSSLIHHQKSH 336
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
230-252 7.72e-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: 7.72e-03
                          10        20
                  ....*....|....*....|...
gi 1622897150 230 YECRECGKTFSHGSSLTRHQISH 252
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
286-308 8.52e-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: 8.52e-03
                          10        20
                  ....*....|....*....|...
gi 1622897150 286 YECMNCGKSFSRVSLLIQHLRIH 308
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
285-332 9.61e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.01  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622897150 285 PYECMNCGKSFSRVSLLIQHLRIHTQEKRyeCRICGKAFIHSSSLIHH 332
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSKV--CPVCGKEFRNTDSTLDH 118
 
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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