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Conserved domains on  [gi|1907124236|ref|XP_036016477|]
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zinc finger protein 57 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-69 3.97e-20

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 3.97e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907124236   12 VSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTFVGSKKKPQEPSSDLQDKNE 69
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 166-187 2.23e-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: 2.23e-03
                          10        20
                  ....*....|....*....|..
gi 1907124236 166 SCPECGKCFRDQSEVNRHLKVH 187
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
136-306 5.25e-03

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


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124236 136 PFFCNFCGKTYRDASGLSRHRRAHL----GYRPRSCPE--CGKCFRDQSEVNRHLKVHQNKPAAsnqagNQASNQRLKSR 209
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPA-----KEKLLNSSSKF 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124236 210 VPPTTPRSQAPALKYVkviqGPVARAKARNSGASTL-------NVRSNSITVVRSREK-ISCPYCHITFTMRTCLLTHLK 281
Cdd:COG5048   364 SPLLNNEPPQSLQQYK----DLKNDKKSETLSNSCIrnfkrdsNLSLHIITHLSFRPYnCKNPPCSKSFNRHYNLIPHKK 439

                         170       180
                  ....*....|....*....|....*...
gi 1907124236 282 IHFRRQPNQHFCCK---ESAHSSNTLRM 306
Cdd:COG5048   440 IHTNHAPLLCSILKsfrRDLDLSNHGKD 467
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-69 3.97e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 3.97e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907124236   12 VSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTFVGSKKKPQEPSSDLQDKNE 69
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 2.23e-17

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: 75.20  E-value: 2.23e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907124236  11 PVSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTFVG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-50 5.92e-14

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: 65.65  E-value: 5.92e-14
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907124236  12 VSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTF 50
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 166-187 2.23e-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: 2.23e-03
                          10        20
                  ....*....|....*....|..
gi 1907124236 166 SCPECGKCFRDQSEVNRHLKVH 187
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
136-306 5.25e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124236 136 PFFCNFCGKTYRDASGLSRHRRAHL----GYRPRSCPE--CGKCFRDQSEVNRHLKVHQNKPAAsnqagNQASNQRLKSR 209
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPA-----KEKLLNSSSKF 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124236 210 VPPTTPRSQAPALKYVkviqGPVARAKARNSGASTL-------NVRSNSITVVRSREK-ISCPYCHITFTMRTCLLTHLK 281
Cdd:COG5048   364 SPLLNNEPPQSLQQYK----DLKNDKKSETLSNSCIrnfkrdsNLSLHIITHLSFRPYnCKNPPCSKSFNRHYNLIPHKK 439

                         170       180
                  ....*....|....*....|....*...
gi 1907124236 282 IHFRRQPNQHFCCK---ESAHSSNTLRM 306
Cdd:COG5048   440 IHTNHAPLLCSILKsfrRDLDLSNHGKD 467
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
12-69 3.97e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 3.97e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907124236   12 VSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTFVGSKKKPQEPSSDLQDKNE 69
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 11-52 2.23e-17

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: 75.20  E-value: 2.23e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907124236  11 PVSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTFVG 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-50 5.92e-14

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: 65.65  E-value: 5.92e-14
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907124236  12 VSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTF 50
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 166-187 2.23e-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: 2.23e-03
                          10        20
                  ....*....|....*....|..
gi 1907124236 166 SCPECGKCFRDQSEVNRHLKVH 187
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
136-306 5.25e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124236 136 PFFCNFCGKTYRDASGLSRHRRAHL----GYRPRSCPE--CGKCFRDQSEVNRHLKVHQNKPAAsnqagNQASNQRLKSR 209
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPA-----KEKLLNSSSKF 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124236 210 VPPTTPRSQAPALKYVkviqGPVARAKARNSGASTL-------NVRSNSITVVRSREK-ISCPYCHITFTMRTCLLTHLK 281
Cdd:COG5048   364 SPLLNNEPPQSLQQYK----DLKNDKKSETLSNSCIrnfkrdsNLSLHIITHLSFRPYnCKNPPCSKSFNRHYNLIPHKK 439

                         170       180
                  ....*....|....*....|....*...
gi 1907124236 282 IHFRRQPNQHFCCK---ESAHSSNTLRM 306
Cdd:COG5048   440 IHTNHAPLLCSILKsfrRDLDLSNHGKD 467
 
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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