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Conserved domains on  [gi|38505215|ref|NP_079316|]
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zinc finger protein 614 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 2.90e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.46  E-value: 2.90e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38505215      8 LTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSLGYQTSKPDVLSKLAHGQEPWT 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-530 2.50e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 369 KPYMCSECGKGFTVKSNLIVHQRS--HTGE--KSYICSE--CGKGFTVKRTLVIHQRTHTGEKSYIC--NECGKGFTTK- 439
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLl 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 440 ----RTLIIHQRTHTGEKPYEC--NECGKAFSQKICLIQHERCHTGKTP--FVCTECGKSYSHKYGLITHQRIHTGEKPY 511
Cdd:COG5048 368 nnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                       170
                ....*....|....*....
gi 38505215 512 ECNECGKAFTTKSVLNVHQ 530
Cdd:COG5048 448 LCSILKSFRRDLDLSNHGK 466
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
92-350 1.47e-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: 41.22  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215  92 SPNQRLLKSVQQCNGQNTLRNIVHLSKTHFPIVQNHDTFDLYRKNLKSSLSLINQKRRHGINN---PVEFIGGEKTLLHG 168
Cdd:COG5048 164 SNSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSlplTTNSQLSPKSLLSQ 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 169 KHERTHTKTRFSENAKCIHTKFQVFKHQRTQKIE----------KPHACIECEQTFLRKSQLIYHENICI--------QE 230
Cdd:COG5048 244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSVNhsgeslkpFS 323

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 231 NPGSGQCEKLSRSVLFTKHLKTNTTDK-------ICIPNEYRKGSTVKSSLITHQQTHTEEKSYMC--SECGKGFTMKRY 301
Cdd:COG5048 324 CPYSLCGKLFSRNDALKRHILLHTSISpakekllNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSN 403

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 38505215 302 LIAHQRTHSGEKPYVCK--ECGKGFTVKSNLIVHQRTHTGEKPYICSECGK 350
Cdd:COG5048 404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 2.90e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.46  E-value: 2.90e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38505215      8 LTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSLGYQTSKPDVLSKLAHGQEPWT 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 1.30e-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: 90.61  E-value: 1.30e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38505215     7 SLTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSLG 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 2.58e-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: 81.06  E-value: 2.58e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 38505215   8 LTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSL 47
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-530 2.50e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 369 KPYMCSECGKGFTVKSNLIVHQRS--HTGE--KSYICSE--CGKGFTVKRTLVIHQRTHTGEKSYIC--NECGKGFTTK- 439
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLl 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 440 ----RTLIIHQRTHTGEKPYEC--NECGKAFSQKICLIQHERCHTGKTP--FVCTECGKSYSHKYGLITHQRIHTGEKPY 511
Cdd:COG5048 368 nnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                       170
                ....*....|....*....
gi 38505215 512 ECNECGKAFTTKSVLNVHQ 530
Cdd:COG5048 448 LCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
498-522 4.27e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.27e-04
                          10        20
                  ....*....|....*....|....*
gi 38505215   498 LITHQRIHTGEKPYECNECGKAFTT 522
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
92-350 1.47e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215  92 SPNQRLLKSVQQCNGQNTLRNIVHLSKTHFPIVQNHDTFDLYRKNLKSSLSLINQKRRHGINN---PVEFIGGEKTLLHG 168
Cdd:COG5048 164 SNSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSlplTTNSQLSPKSLLSQ 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 169 KHERTHTKTRFSENAKCIHTKFQVFKHQRTQKIE----------KPHACIECEQTFLRKSQLIYHENICI--------QE 230
Cdd:COG5048 244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSVNhsgeslkpFS 323

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 231 NPGSGQCEKLSRSVLFTKHLKTNTTDK-------ICIPNEYRKGSTVKSSLITHQQTHTEEKSYMC--SECGKGFTMKRY 301
Cdd:COG5048 324 CPYSLCGKLFSRNDALKRHILLHTSISpakekllNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSN 403

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 38505215 302 LIAHQRTHSGEKPYVCK--ECGKGFTVKSNLIVHQRTHTGEKPYICSECGK 350
Cdd:COG5048 404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 315-337 4.58e-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: 4.58e-03
                          10        20
                  ....*....|....*....|...
gi 38505215   315 YVCKECGKGFTVKSNLIVHQRTH 337
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 2.90e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 118.46  E-value: 2.90e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38505215      8 LTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSLGYQTSKPDVLSKLAHGQEPWT 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 1.30e-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: 90.61  E-value: 1.30e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 38505215     7 SLTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSLG 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 2.58e-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: 81.06  E-value: 2.58e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 38505215   8 LTLEDVAVEFSWEEWQLLDTAQKNLYRDVMVENYNHLVSL 47
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-530 2.50e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 369 KPYMCSECGKGFTVKSNLIVHQRS--HTGE--KSYICSE--CGKGFTVKRTLVIHQRTHTGEKSYIC--NECGKGFTTK- 439
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLl 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 440 ----RTLIIHQRTHTGEKPYEC--NECGKAFSQKICLIQHERCHTGKTP--FVCTECGKSYSHKYGLITHQRIHTGEKPY 511
Cdd:COG5048 368 nnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                       170
                ....*....|....*....
gi 38505215 512 ECNECGKAFTTKSVLNVHQ 530
Cdd:COG5048 448 LCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
498-522 4.27e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.27e-04
                          10        20
                  ....*....|....*....|....*
gi 38505215   498 LITHQRIHTGEKPYECNECGKAFTT 522
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-466 5.85e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.85e-04
                          10        20
                  ....*....|....*....|..
gi 38505215   445 HQRTHTGEKPYECNECGKAFSQ 466
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
92-350 1.47e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215  92 SPNQRLLKSVQQCNGQNTLRNIVHLSKTHFPIVQNHDTFDLYRKNLKSSLSLINQKRRHGINN---PVEFIGGEKTLLHG 168
Cdd:COG5048 164 SNSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSlplTTNSQLSPKSLLSQ 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 169 KHERTHTKTRFSENAKCIHTKFQVFKHQRTQKIE----------KPHACIECEQTFLRKSQLIYHENICI--------QE 230
Cdd:COG5048 244 SPSSLSSSDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSVNhsgeslkpFS 323

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38505215 231 NPGSGQCEKLSRSVLFTKHLKTNTTDK-------ICIPNEYRKGSTVKSSLITHQQTHTEEKSYMC--SECGKGFTMKRY 301
Cdd:COG5048 324 CPYSLCGKLFSRNDALKRHILLHTSISpakekllNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSN 403

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 38505215 302 LIAHQRTHSGEKPYVCK--ECGKGFTVKSNLIVHQRTHTGEKPYICSECGK 350
Cdd:COG5048 404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
357-381 3.29e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.29e-03
                          10        20
                  ....*....|....*....|....*
gi 38505215   357 YLVVHQRTHTGEKPYMCSECGKGFT 381
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 315-337 4.58e-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: 4.58e-03
                          10        20
                  ....*....|....*....|...
gi 38505215   315 YVCKECGKGFTVKSNLIVHQRTH 337
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 511-533 7.40e-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: 34.20  E-value: 7.40e-03
                          10        20
                  ....*....|....*....|...
gi 38505215   511 YECNECGKAFTTKSVLNVHQRTH 533
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
301-325 8.05e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.05e-03
                          10        20
                  ....*....|....*....|....*
gi 38505215   301 YLIAHQRTHSGEKPYVCKECGKGFT 325
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
 
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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