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Conserved domains on  [gi|1912229888|ref|NP_001374226|]
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zinc finger protein 133 isoform n [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-63 1.44e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.32  E-value: 1.44e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888    4 MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLGISFSKPELITQLEQGKETW 63
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-626 6.03e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.81  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 217 NCGECGLSFSKMTNLLSHQRIHSGEKPYVCGV--CEKGFSLKKSLARHQKAHSGEKPIVC--RECGRGFNRKSTLIIHER 292
Cdd:COG5048    35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLSSSS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 293 THSgekPYMCSECGRGFSQKSNLIIHqrtHSGEKPYVCRECGKGFSQKSAVVRHQRTHLEEKTIVCSDCGLGFSDRSNLI 372
Cdd:COG5048   115 SNS---NDNNLLSSHSLPPSSRDPQL---PDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 373 SHQRTHSGEKPYACKECGRcFRQRTTLVNHQRTHSKEKPYVCGVCGHSFSQNSTLISHRRTHTGEKPYVCGVCGRGFSLK 452
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 453 SHLNRHQNIHSGE-------KPIVCKDCGRGFSQQSNLIRHQRT--HSGE--KPMVCGE--CGRGFSQKSNLVAHQRTHS 519
Cdd:COG5048   268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 520 GERPYVCRECGRGFSHQ-------AGLIRHKRKHSREKPYMC--RQCGLGFGNKSALITHKRAHSEEKPCVCRECGQGFL 590
Cdd:COG5048   348 SISPAKEKLLNSSSKFSpllnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKS 427

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1912229888 591 QKSHLTL--HQMTHTGEKPYVCKTCGRgFSLKSHLSRH 626
Cdd:COG5048   428 FNRHYNLipHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-63 1.44e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.32  E-value: 1.44e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888    4 MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLGISFSKPELITQLEQGKETW 63
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 4-44 8.12e-24

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: 94.07  E-value: 8.12e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1912229888   4 MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLG 44
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-43 1.34e-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: 82.21  E-value: 1.34e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1912229888   4 MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSL 43
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-626 6.03e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.81  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 217 NCGECGLSFSKMTNLLSHQRIHSGEKPYVCGV--CEKGFSLKKSLARHQKAHSGEKPIVC--RECGRGFNRKSTLIIHER 292
Cdd:COG5048    35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLSSSS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 293 THSgekPYMCSECGRGFSQKSNLIIHqrtHSGEKPYVCRECGKGFSQKSAVVRHQRTHLEEKTIVCSDCGLGFSDRSNLI 372
Cdd:COG5048   115 SNS---NDNNLLSSHSLPPSSRDPQL---PDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 373 SHQRTHSGEKPYACKECGRcFRQRTTLVNHQRTHSKEKPYVCGVCGHSFSQNSTLISHRRTHTGEKPYVCGVCGRGFSLK 452
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 453 SHLNRHQNIHSGE-------KPIVCKDCGRGFSQQSNLIRHQRT--HSGE--KPMVCGE--CGRGFSQKSNLVAHQRTHS 519
Cdd:COG5048   268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 520 GERPYVCRECGRGFSHQ-------AGLIRHKRKHSREKPYMC--RQCGLGFGNKSALITHKRAHSEEKPCVCRECGQGFL 590
Cdd:COG5048   348 SISPAKEKLLNSSSKFSpllnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKS 427

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1912229888 591 QKSHLTL--HQMTHTGEKPYVCKTCGRgFSLKSHLSRH 626
Cdd:COG5048   428 FNRHYNLipHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
370-395 7.36e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.36e-04
                          10        20
                  ....*....|....*....|....*.
gi 1912229888 370 NLISHQRTHSGEKPYACKECGRCFRQ 395
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-63 1.44e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.32  E-value: 1.44e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888    4 MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLGISFSKPELITQLEQGKETW 63
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 4-44 8.12e-24

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: 94.07  E-value: 8.12e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1912229888   4 MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLG 44
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-43 1.34e-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: 82.21  E-value: 1.34e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1912229888   4 MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSL 43
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-626 6.03e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.81  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 217 NCGECGLSFSKMTNLLSHQRIHSGEKPYVCGV--CEKGFSLKKSLARHQKAHSGEKPIVC--RECGRGFNRKSTLIIHER 292
Cdd:COG5048    35 SCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLSSSS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 293 THSgekPYMCSECGRGFSQKSNLIIHqrtHSGEKPYVCRECGKGFSQKSAVVRHQRTHLEEKTIVCSDCGLGFSDRSNLI 372
Cdd:COG5048   115 SNS---NDNNLLSSHSLPPSSRDPQL---PDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 373 SHQRTHSGEKPYACKECGRcFRQRTTLVNHQRTHSKEKPYVCGVCGHSFSQNSTLISHRRTHTGEKPYVCGVCGRGFSLK 452
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 453 SHLNRHQNIHSGE-------KPIVCKDCGRGFSQQSNLIRHQRT--HSGE--KPMVCGE--CGRGFSQKSNLVAHQRTHS 519
Cdd:COG5048   268 ASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 520 GERPYVCRECGRGFSHQ-------AGLIRHKRKHSREKPYMC--RQCGLGFGNKSALITHKRAHSEEKPCVCRECGQGFL 590
Cdd:COG5048   348 SISPAKEKLLNSSSKFSpllnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKS 427

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1912229888 591 QKSHLTL--HQMTHTGEKPYVCKTCGRgFSLKSHLSRH 626
Cdd:COG5048   428 FNRHYNLipHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
298-646 7.65e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 7.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 298 KPYMCSECGRGFSQKSNLIIHQRTHSGEKPYVCR--ECGKGFSQKSAVVRHQRTHLEEKTIVCSDCGLG--FSDRSNLIS 373
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLsnSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 374 HQRTHSgEKPYACKECGRCFRQRTTLVNHQRTHSKEKPYVCGVCGHSFSQ----NSTLISHRRTHTGEKPYVCgvcgrgf 449
Cdd:COG5048   112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsNSLHPPLPANSLSKDPSSN------- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 450 slkSHLNRHQNIHSGEKPIVCKDCGRGFSQQSNLIRHQRTHSGEKPMVCGECGRGFSQKSNLVAHQRTHSGERPYVCREC 529
Cdd:COG5048   184 ---LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 530 GRGFSHQAGLIRHKRKHS-------REKPYMCRQCGLGFGNKSALITHKRA--HSEE--KPCVCRE--CGQGFLQKSHLT 596
Cdd:COG5048   261 PRSSLPTASSQSSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALK 340

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1912229888 597 LHQMTHTGEKPYVCKTCGRGfSLKSHLSRHRKTTSVHHRLPVQPDPEPCA 646
Cdd:COG5048   341 RHILLHTSISPAKEKLLNSS-SKFSPLLNNEPPQSLQQYKDLKNDKKSET 389
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
418-498 1.18e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912229888 418 GHSFSQNSTLISHRRTHT------GEKPYVCGVCGRGFSLKSHLNRHQNIHSGEKPIVCKDCGRG--FSQQSNLIRHQRT 489
Cdd:COG5048     6 SQSSSSNNSVLSSTPKSTlkslsnAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRT 85


                  ....*....
gi 1912229888 490 HSGEKPMVC 498
Cdd:COG5048    86 HHNNPSDLN 94
zf-H2C2_2 pfam13465
Zinc-finger double domain;
370-395 7.36e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.36e-04
                          10        20
                  ....*....|....*....|....*.
gi 1912229888 370 NLISHQRTHSGEKPYACKECGRCFRQ 395
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
314-339 1.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|....*.
gi 1912229888 314 NLIIHQRTHSGEKPYVCRECGKGFSQ 339
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 469-490 1.27e-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: 36.51  E-value: 1.27e-03
                          10        20
                  ....*....|....*....|..
gi 1912229888 469 VCKDCGRGFSQQSNLIRHQRTH 490
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 300-322 1.33e-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: 36.51  E-value: 1.33e-03
                          10        20
                  ....*....|....*....|...
gi 1912229888 300 YMCSECGRGFSQKSNLIIHQRTH 322
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
230-254 4.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.14e-03
                          10        20
                  ....*....|....*....|....*
gi 1912229888 230 NLLSHQRIHSGEKPYVCGVCEKGFS 254
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
510-535 5.30e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.30e-03
                          10        20
                  ....*....|....*....|....*.
gi 1912229888 510 NLVAHQRTHSGERPYVCRECGRGFSH 535
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 384-406 7.65e-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: 7.65e-03
                          10        20
                  ....*....|....*....|...
gi 1912229888 384 YACKECGRCFRQRTTLVNHQRTH 406
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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