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Conserved domains on  [gi|121583782|ref|NP_001073412|]
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zinc finger protein 426 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
40-97 6.76e-28

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 6.76e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 121583782    40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVGYQLIKPSVISWLEQEEF 97
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-483 4.32e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 331 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 402
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 403 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 471
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445

                        170
                 ....*....|..
gi 121583782 472 PYECKQCGKAFS 483
Cdd:COG5048  446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
291-316 1.18e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.18e-05
                          10        20
                  ....*....|....*....|....*.
gi 121583782  291 YLNIHMRTHTGEKPYECKECGKAFNY 316
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
487-512 1.90e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.90e-04
                          10        20
                  ....*....|....*....|....*.
gi 121583782  487 SFQIHERTHTGEKPYECKECGKAFIC 512
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 222-244 5.10e-04

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: 37.28  E-value: 5.10e-04
                          10        20
                  ....*....|....*....|...
gi 121583782  222 FECSDCGKSFMNQSHLQTHQRTH 244
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
40-97 6.76e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 6.76e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 121583782    40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVGYQLIKPSVISWLEQEEF 97
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 39-80 2.10e-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: 87.14  E-value: 2.10e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 121583782   39 LVSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVG 80
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 40-77 3.87e-16

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: 72.20  E-value: 3.87e-16
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 121583782  40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLA 77
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-483 4.32e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 331 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 402
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 403 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 471
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445

                        170
                 ....*....|..
gi 121583782 472 PYECKQCGKAFS 483
Cdd:COG5048  446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
459-484 4.81e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 4.81e-06
                          10        20
                  ....*....|....*....|....*.
gi 121583782  459 HLKIHMRIHTGEKPYECKQCGKAFSH 484
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
291-316 1.18e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.18e-05
                          10        20
                  ....*....|....*....|....*.
gi 121583782  291 YLNIHMRTHTGEKPYECKECGKAFNY 316
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
487-512 1.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.90e-04
                          10        20
                  ....*....|....*....|....*.
gi 121583782  487 SFQIHERTHTGEKPYECKECGKAFIC 512
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 222-244 5.10e-04

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: 37.28  E-value: 5.10e-04
                          10        20
                  ....*....|....*....|...
gi 121583782  222 FECSDCGKSFMNQSHLQTHQRTH 244
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
40-97 6.76e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 6.76e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 121583782    40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVGYQLIKPSVISWLEQEEF 97
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 39-80 2.10e-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: 87.14  E-value: 2.10e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 121583782   39 LVSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVG 80
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 40-77 3.87e-16

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: 72.20  E-value: 3.87e-16
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 121583782  40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLA 77
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
331-483 4.32e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 331 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 402
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 403 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 471
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445

                        170
                 ....*....|..
gi 121583782 472 PYECKQCGKAFS 483
Cdd:COG5048  446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
459-484 4.81e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 4.81e-06
                          10        20
                  ....*....|....*....|....*.
gi 121583782  459 HLKIHMRIHTGEKPYECKQCGKAFSH 484
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
218-553 5.08e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.92  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 218 QEKCFECSDCGKSFMNQSHLQTHQRTHSGDKLYELNECGRSFINSRLAVLIETLNAKKPHR----CKECGKGYRYPAYLN 293
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPsdlnSKSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 294 IHMRTHTGEKPYECKECGKAFNYSNSFQIHGRTHT---GEKPYVCNQCGKAFTQHSGLSIHVRSHNGDKPyacKECGKAF 370
Cdd:COG5048  110 LSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKD---PSSNLSL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 371 LTSSRLIQHIRTHTgekpfVCVKCGKAFAISSNLNGHLKMHAEEKT-CECKICGKAFGYLSCLNNHM----RTHNAKKSY 445
Cdd:COG5048  187 LISSNVSTSIPSSS-----ENSPLSSSYSIPSSSSDQNLENSSSSLpLTTNSQLSPKSLLSQSPSSLsssdSSSSASESP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 446 TCKECGKAFNYSTHLKIHMRIHTG-EKPYECKQCGKAFSHSTSFQIHERT--HTGE--KPYECKE--CGKAFICPSSFRI 518
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 121583782 519 HEISHTHTEEKPYKCQQCGKAYSHPRSLRRHERIH 553
Cdd:COG5048  342 HILLHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
291-316 1.18e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.18e-05
                          10        20
                  ....*....|....*....|....*.
gi 121583782  291 YLNIHMRTHTGEKPYECKECGKAFNY 316
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
272-553 3.78e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 272 NAKKPHRCKECGKGYRYPAYLNIHMRTHTGEKPYECKECGKAFNYSN--SFQIHGRTHTGEKPYVCN-QCGKAFTQHSGL 348
Cdd:COG5048   29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRplELSRHLRTHHNNPSDLNSkSLPLSNSKASSS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 349 SIHVRSHNGDKPYACKECGKAFLTSSRLIQHIRTHT-------GEKPFVCVKCGKAFAISSNLNGHLKMHAEEKTCECKI 421
Cdd:COG5048  109 SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrnnplPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121583782 422 CG-KAFGYLSCLNNHMRTHNAKKSYTCKECGKaFNYSTHLKIHMRIHTGEK------------PYECKQCGKAFSHSTSF 488
Cdd:COG5048  189 SSnVSTSIPSSSENSPLSSSYSIPSSSSDQNL-ENSSSSLPLTTNSQLSPKsllsqspsslssSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121583782 489 QIHERTH----------TGEKPYECKECGKAFICPSSFRIHEISHTHTEE--KPYKC--QQCGKAYSHPRSLRRHERIH 553
Cdd:COG5048  268 ASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346
zf-H2C2_2 pfam13465
Zinc-finger double domain;
487-512 1.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.90e-04
                          10        20
                  ....*....|....*....|....*.
gi 121583782  487 SFQIHERTHTGEKPYECKECGKAFIC 512
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 222-244 5.10e-04

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: 37.28  E-value: 5.10e-04
                          10        20
                  ....*....|....*....|...
gi 121583782  222 FECSDCGKSFMNQSHLQTHQRTH 244
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 445-467 1.37e-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: 36.12  E-value: 1.37e-03
                          10        20
                  ....*....|....*....|...
gi 121583782  445 YTCKECGKAFNYSTHLKIHMRIH 467
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
432-456 3.47e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.47e-03
                          10        20
                  ....*....|....*....|....*
gi 121583782  432 LNNHMRTHNAKKSYTCKECGKAFNY 456
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
375-399 4.80e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.80e-03
                          10        20
                  ....*....|....*....|....*
gi 121583782  375 RLIQHIRTHTGEKPFVCVKCGKAFA 399
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
319-344 7.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.11e-03
                          10        20
                  ....*....|....*....|....*.
gi 121583782  319 SFQIHGRTHTGEKPYVCNQCGKAFTQ 344
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-372 7.54e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.54e-03
                          10        20
                  ....*....|....*....|....*
gi 121583782  348 LSIHVRSHNGDKPYACKECGKAFLT 372
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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