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Conserved domains on  [gi|1958798011|ref|XP_038938100|]
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zinc finger protein 426 isoform X3 [Rattus norvegicus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204728)

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; similar to Homo sapiens zinc finger protein 426

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
40-97 6.73e-28

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 6.73e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798011   40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLATVGYQLIKPSVISWLEQEEF 97
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
330-482 4.12e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 330 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 401
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 402 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 470
Cdd:COG5048   368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445
                         170
                  ....*....|..
gi 1958798011 471 PYECKQCGKAFS 482
Cdd:COG5048   446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-315 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 1958798011 290 YLNIHMRTHTGEKPYECKECGKAFNY 315
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
486-511 1.88e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.88e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958798011 486 SFQIHERTHTGEKPYECKECGKAFIC 511
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
221-243 5.09e-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: 5.09e-04
                          10        20
                  ....*....|....*....|...
gi 1958798011 221 FECSDCGKSFMNQSHLQTHQRTH 243
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
40-97 6.73e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 6.73e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798011   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 1958798011  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 3.86e-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: 3.86e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958798011  40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLA 77
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
330-482 4.12e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 330 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 401
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 402 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 470
Cdd:COG5048   368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445
                         170
                  ....*....|..
gi 1958798011 471 PYECKQCGKAFS 482
Cdd:COG5048   446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-483 4.85e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 4.85e-06
                          10        20
                  ....*....|....*....|....*.
gi 1958798011 458 HLKIHMRIHTGEKPYECKQCGKAFSH 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-315 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 1958798011 290 YLNIHMRTHTGEKPYECKECGKAFNY 315
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
486-511 1.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.88e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958798011 486 SFQIHERTHTGEKPYECKECGKAFIC 511
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
221-243 5.09e-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: 5.09e-04
                          10        20
                  ....*....|....*....|...
gi 1958798011 221 FECSDCGKSFMNQSHLQTHQRTH 243
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
40-97 6.73e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 105.75  E-value: 6.73e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798011   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 1958798011  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 3.86e-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: 3.86e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958798011  40 VSFDDVIVDFTQEEWTSLNPDQRTLYREVMLENYKNLA 77
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
330-482 4.12e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 330 KPYVCNQCGKAFTQHSGLSIHVRSHN----GDKPYACKE--CGKAFLTSSRLIQHIRTHTGEKPFVCV--KCGKAFAISS 401
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 402 NLNGHLKMHAEEKTCECKICGKAfgYLSCLNNHMRTHNAKKS-----------YTCKECGKAFNYSTHLKIHMRIHTGEK 470
Cdd:COG5048   368 NNEPPQSLQQYKDLKNDKKSETL--SNSCIRNFKRDSNLSLHiithlsfrpynCKNPPCSKSFNRHYNLIPHKKIHTNHA 445
                         170
                  ....*....|..
gi 1958798011 471 PYECKQCGKAFS 482
Cdd:COG5048   446 PLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-483 4.85e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 4.85e-06
                          10        20
                  ....*....|....*....|....*.
gi 1958798011 458 HLKIHMRIHTGEKPYECKQCGKAFSH 483
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-552 4.89e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 217 QEKCFECSDCGKSFMNQSHLQTHQRTHSGDKLYELNECGRSFINSRLAVLIETLNAKKPHR----CKECGKGYRYPAYLN 292
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPsdlnSKSLPLSNSKASSSS 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 293 IHMRTHTGEKPYECKECGKAFNYSNSFQIHGRTHT---GEKPYVCNQCGKAFTQHSGLSIHVRSHNGDKPyacKECGKAF 369
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKD---PSSNLSL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 370 LTSSRLIQHIRTHTgekpfVCVKCGKAFAISSNLNGHLKMHAEEKT-CECKICGKAFGYLSCLNNHM----RTHNAKKSY 444
Cdd:COG5048   187 LISSNVSTSIPSSS-----ENSPLSSSYSIPSSSSDQNLENSSSSLpLTTNSQLSPKSLLSQSPSSLsssdSSSSASESP 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 445 TCKECGKAFNYSTHLKIHMRIHTG-EKPYECKQCGKAFSHSTSFQIHERT--HTGE--KPYECKE--CGKAFICPSSFRI 517
Cdd:COG5048   262 RSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKR 341
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1958798011 518 HEISHTHTEEKPYKCQQCGKAYSHPRSLRRHERIH 552
Cdd:COG5048   342 HILLHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-315 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 1958798011 290 YLNIHMRTHTGEKPYECKECGKAFNY 315
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
271-552 3.64e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 271 NAKKPHRCKECGKGYRYPAYLNIHMRTHTGEKPYECKECGKAFNYSN--SFQIHGRTHTGEKPYVCN-QCGKAFTQHSGL 347
Cdd:COG5048    29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRplELSRHLRTHHNNPSDLNSkSLPLSNSKASSS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 348 SIHVRSHNGDKPYACKECGKAFLTSSRLIQHIRTHT-------GEKPFVCVKCGKAFAISSNLNGHLKMHAEEKTCECKI 420
Cdd:COG5048   109 SLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlrnnplPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798011 421 CG-KAFGYLSCLNNHMRTHNAKKSYTCKECGKaFNYSTHLKIHMRIHTGEK------------PYECKQCGKAFSHSTSF 487
Cdd:COG5048   189 SSnVSTSIPSSSENSPLSSSYSIPSSSSDQNL-ENSSSSLPLTTNSQLSPKsllsqspsslssSDSSSSASESPRSSLPT 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798011 488 QIHERTH----------TGEKPYECKECGKAFICPSSFRIHEISHTHTEE--KPYKC--QQCGKAYSHPRSLRRHERIH 552
Cdd:COG5048   268 ASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLH 346
zf-H2C2_2 pfam13465
Zinc-finger double domain;
486-511 1.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.88e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958798011 486 SFQIHERTHTGEKPYECKECGKAFIC 511
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
221-243 5.09e-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: 5.09e-04
                          10        20
                  ....*....|....*....|...
gi 1958798011 221 FECSDCGKSFMNQSHLQTHQRTH 243
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
444-466 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 1958798011 444 YTCKECGKAFNYSTHLKIHMRIH 466
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
431-455 3.50e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.50e-03
                          10        20
                  ....*....|....*....|....*
gi 1958798011 431 LNNHMRTHNAKKSYTCKECGKAFNY 455
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
374-398 4.79e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.79e-03
                          10        20
                  ....*....|....*....|....*
gi 1958798011 374 RLIQHIRTHTGEKPFVCVKCGKAFA 398
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
318-343 7.03e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.03e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958798011 318 SFQIHGRTHTGEKPYVCNQCGKAFTQ 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
347-371 7.46e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.46e-03
                          10        20
                  ....*....|....*....|....*
gi 1958798011 347 LSIHVRSHNGDKPYACKECGKAFLT 371
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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