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Conserved domains on  [gi|672061052|ref|XP_008764206|]
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zinc finger protein 426 isoform X5 [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;
14-71 5.89e-28

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 5.89e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 672061052    14 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVGYQLIKPSVISWLEQEEF 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
305-457 3.80e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 305 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 376
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 377 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 445
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445

                        170
                 ....*....|..
gi 672061052 446 PYECKQCGKAFS 457
Cdd:COG5048  446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
265-290 1.52e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.52e-05
                          10        20
                  ....*....|....*....|....*.
gi 672061052  265 YLNIHMRTHTGEKPYECKECGKAFNY 290
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
461-486 2.38e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 672061052  461 SFQIHERTHTGEKPYECKECGKAFIC 486
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 196-218 6.73e-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: 36.89  E-value: 6.73e-04
                          10        20
                  ....*....|....*....|...
gi 672061052  196 FECSDCGKSFMNQSHLQTHQRTH 218
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-71 5.89e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 5.89e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 672061052    14 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVGYQLIKPSVISWLEQEEF 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 1.97e-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: 1.97e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 672061052   13 LVSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-51 3.69e-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: 3.69e-16
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 672061052  14 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLA 51
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
305-457 3.80e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 305 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 376
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 377 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 445
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445

                        170
                 ....*....|..
gi 672061052 446 PYECKQCGKAFS 457
Cdd:COG5048  446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-458 6.22e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.22e-06
                          10        20
                  ....*....|....*....|....*.
gi 672061052  433 HLKIHMRIHTGEKPYECKQCGKAFSH 458
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
265-290 1.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.52e-05
                          10        20
                  ....*....|....*....|....*.
gi 672061052  265 YLNIHMRTHTGEKPYECKECGKAFNY 290
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
461-486 2.38e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 672061052  461 SFQIHERTHTGEKPYECKECGKAFIC 486
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 196-218 6.73e-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: 36.89  E-value: 6.73e-04
                          10        20
                  ....*....|....*....|...
gi 672061052  196 FECSDCGKSFMNQSHLQTHQRTH 218
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-71 5.89e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 5.89e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 672061052    14 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVGYQLIKPSVISWLEQEEF 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 1.97e-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: 1.97e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 672061052   13 LVSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-51 3.69e-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: 3.69e-16
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 672061052  14 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLA 51
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
305-457 3.80e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 305 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 376
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 377 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 445
Cdd:COG5048  368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445

                        170
                 ....*....|..
gi 672061052 446 PYECKQCGKAFS 457
Cdd:COG5048  446 PLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-527 4.52e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 192 QEKCFECSDCGKSFMNQSHLQTHQRTHSGDKLYELNECGRSFINSRLAVLIETLNAKKPHR----CKECGKGYRYPAYLN 267
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPsdlnSKSLPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 268 IHMRTHTGEKPYECKECGKAFNYSNSFQIHGRTHT---GEKPYVCNQCGKAFTQHSGLSIHVRSHNGDKPyacKECGKAF 344
Cdd:COG5048  110 LSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKD---PSSNLSL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 345 LTSSRLIQHIRTHTgekpfVCVKCGKAFAISSNLNGHLKMHAEEKT-CECKICGKAFGYLSCLNNHM----RTHNAKKSY 419
Cdd:COG5048  187 LISSNVSTSIPSSS-----ENSPLSSSYSIPSSSSDQNLENSSSSLpLTTNSQLSPKSLLSQSPSSLsssdSSSSASESP 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 420 TCKECGKAFNYSTHLKIHMRIHTG-EKPYECKQCGKAFSHSTSFQIHERT--HTGE--KPYECKE--CGKAFICPSSFRI 492
Cdd:COG5048  262 RSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 672061052 493 HEISHTHTEEKPYKCQQCGKAYSHPRSLRRHERIH 527
Cdd:COG5048  342 HILLHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-458 6.22e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.22e-06
                          10        20
                  ....*....|....*....|....*.
gi 672061052  433 HLKIHMRIHTGEKPYECKQCGKAFSH 458
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
265-290 1.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.52e-05
                          10        20
                  ....*....|....*....|....*.
gi 672061052  265 YLNIHMRTHTGEKPYECKECGKAFNY 290
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
246-527 3.35e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 246 NAKKPHRCKECGKGYRYPAYLNIHMRTHTGEKPYECKECGKAFNYSN--SFQIHGRTHTGEKPYVCN-QCGKAFTQHSGL 322
Cdd:COG5048   29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRplELSRHLRTHHNNPSDLNSkSLPLSNSKASSS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 323 SIHVRSHNGDKPYACKECGKAFLTSSRLIQHIRTHT-------GEKPFVCVKCGKAFAISSNLNGHLKMHAEEKTCECKI 395
Cdd:COG5048  109 SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrnnplPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672061052 396 CG-KAFGYLSCLNNHMRTHNAKKSYTCKECGKaFNYSTHLKIHMRIHTGEK------------PYECKQCGKAFSHSTSF 462
Cdd:COG5048  189 SSnVSTSIPSSSENSPLSSSYSIPSSSSDQNL-ENSSSSLPLTTNSQLSPKsllsqspsslssSDSSSSASESPRSSLPT 267

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672061052 463 QIHERTH----------TGEKPYECKECGKAFICPSSFRIHEISHTHTEE--KPYKC--QQCGKAYSHPRSLRRHERIH 527
Cdd:COG5048  268 ASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346
zf-H2C2_2 pfam13465
Zinc-finger double domain;
461-486 2.38e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 672061052  461 SFQIHERTHTGEKPYECKECGKAFIC 486
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 196-218 6.73e-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: 36.89  E-value: 6.73e-04
                          10        20
                  ....*....|....*....|...
gi 672061052  196 FECSDCGKSFMNQSHLQTHQRTH 218
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 419-441 1.79e-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: 35.74  E-value: 1.79e-03
                          10        20
                  ....*....|....*....|...
gi 672061052  419 YTCKECGKAFNYSTHLKIHMRIH 441
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
406-430 4.27e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.27e-03
                          10        20
                  ....*....|....*....|....*
gi 672061052  406 LNNHMRTHNAKKSYTCKECGKAFNY 430
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-373 5.74e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 5.74e-03
                          10        20
                  ....*....|....*....|....*
gi 672061052  349 RLIQHIRTHTGEKPFVCVKCGKAFA 373
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
293-318 8.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.76e-03
                          10        20
                  ....*....|....*....|....*.
gi 672061052  293 SFQIHGRTHTGEKPYVCNQCGKAFTQ 318
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
322-346 9.11e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.11e-03
                          10        20
                  ....*....|....*....|....*
gi 672061052  322 LSIHVRSHNGDKPYACKECGKAFLT 346
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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