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Conserved domains on  [gi|112983683|ref|NP_689688|]
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zinc finger protein 417 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
15-55 5.52e-22

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


:

Pssm-ID: 460171  Cd Length: 42  Bit Score: 88.68  E-value: 5.52e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 112983683   15 VTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLG 55
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-568 3.30e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 273 CGKSYSRKSSLIQHQRVHTGKTAYPCEECgKSFSQKGSLISHQRVHTGERPYECREYgkSFGQKGNLIQHQQGHTGERAY 352
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPL-SSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSDS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 353 --HCGECGKSFRQK--FCFINHQRVHTGER-----PYKCGECGKSFGQKGNLVQHQRG--HTGE--RPYECKE--CGKSF 417
Cdd:COG5048  254 ssSASESPRSSLPTasSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 418 RYRSHLTEHQRLHTGERPYNC--RECGKLFNRKYHLLVHERVHtgerpyacevcgklfgnkncvtiHQRIHTGERPYEC- 494
Cdd:COG5048  334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ-----------------------QYKDLKNDKKSETl 390
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112983683 495 -NECGKSFLSSSALHVHKRVHSGQKP--YKCSECGKSFAECSSLIKHRRIHTGERPYECTKCGKTFQRSSTLLHHQS 568
Cdd:COG5048  391 sNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
15-55 5.52e-22

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 88.68  E-value: 5.52e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 112983683   15 VTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLG 55
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
15-70 7.38e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 77.63  E-value: 7.38e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 112983683    15 VTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLGCwCGSKDEEAPCKQR 70
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF-QVPKPDLISQLEQ 55
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
15-54 8.36e-15

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: 68.34  E-value: 8.36e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 112983683  15 VTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSL 54
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-568 3.30e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 273 CGKSYSRKSSLIQHQRVHTGKTAYPCEECgKSFSQKGSLISHQRVHTGERPYECREYgkSFGQKGNLIQHQQGHTGERAY 352
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPL-SSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSDS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 353 --HCGECGKSFRQK--FCFINHQRVHTGER-----PYKCGECGKSFGQKGNLVQHQRG--HTGE--RPYECKE--CGKSF 417
Cdd:COG5048  254 ssSASESPRSSLPTasSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 418 RYRSHLTEHQRLHTGERPYNC--RECGKLFNRKYHLLVHERVHtgerpyacevcgklfgnkncvtiHQRIHTGERPYEC- 494
Cdd:COG5048  334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ-----------------------QYKDLKNDKKSETl 390
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112983683 495 -NECGKSFLSSSALHVHKRVHSGQKP--YKCSECGKSFAECSSLIKHRRIHTGERPYECTKCGKTFQRSSTLLHHQS 568
Cdd:COG5048  391 sNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
394-419 7.57e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.57e-04
                          10        20
                  ....*....|....*....|....*.
gi 112983683  394 NLVQHQRGHTGERPYECKECGKSFRY 419
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
15-55 5.52e-22

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 88.68  E-value: 5.52e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 112983683   15 VTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLG 55
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
15-70 7.38e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 77.63  E-value: 7.38e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 112983683    15 VTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLGCwCGSKDEEAPCKQR 70
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF-QVPKPDLISQLEQ 55
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
15-54 8.36e-15

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: 68.34  E-value: 8.36e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 112983683  15 VTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSL 54
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-568 3.30e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 273 CGKSYSRKSSLIQHQRVHTGKTAYPCEECgKSFSQKGSLISHQRVHTGERPYECREYgkSFGQKGNLIQHQQGHTGERAY 352
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPL-SSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSDS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 353 --HCGECGKSFRQK--FCFINHQRVHTGER-----PYKCGECGKSFGQKGNLVQHQRG--HTGE--RPYECKE--CGKSF 417
Cdd:COG5048  254 ssSASESPRSSLPTasSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLF 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 418 RYRSHLTEHQRLHTGERPYNC--RECGKLFNRKYHLLVHERVHtgerpyacevcgklfgnkncvtiHQRIHTGERPYEC- 494
Cdd:COG5048  334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQ-----------------------QYKDLKNDKKSETl 390
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112983683 495 -NECGKSFLSSSALHVHKRVHSGQKP--YKCSECGKSFAECSSLIKHRRIHTGERPYECTKCGKTFQRSSTLLHHQS 568
Cdd:COG5048  391 sNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
250-483 1.07e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 250 SRYVSFSNHQRDHTAKgpyDCGECGKSYSRKSSLIQ---HQRVHTGKTA-YPCEECGKSFSQKGSLISHQR--VHTGE-- 321
Cdd:COG5048  243 QSPSSLSSSDSSSSAS---ESPRSSLPTASSQSSSPnesDSSSEKGFSLpIKSKQCNISFSRSSPLTRHLRsvNHSGEsl 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 322 RPYECRE--YGKSFGQKGNLIQHQQGHTGERAYHC--GECGKSFRQKFCFINHQRVhtgerpykcgecgksfgqkgnlvQ 397
Cdd:COG5048  320 KPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSL-----------------------Q 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 398 HQRGHTGERPYEC--KECGKSFRYRSHLTEHQRLHTGERPYNCR--ECGKLFNRKYHLLVHERVHTGERPYACEVCGKLF 473
Cdd:COG5048  377 QYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
                        250
                 ....*....|
gi 112983683 474 GNKNCVTIHQ 483
Cdd:COG5048  457 RDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
203-570 1.88e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 203 PPFQEGKTNYSCGKRTKAFS-----TKHSVIP-HQKLFTrdgCYVCSdCGKSFSRYVSFSNHQRDHTAKGPYDCgeCGKS 276
Cdd:COG5048   25 KSLSNAPRPDSCPNCTDSFSrlehlTRHIRSHtGEKPSQ---CSYSG-CDKSFSRPLELSRHLRTHHNNPSDLN--SKSL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 277 YSRKSSLIQHQRVHTGKT---AYPCEECGKSFSQKGSLISHQRVHTGERPYECREYGKSFG------------------- 334
Cdd:COG5048   99 PLSNSKASSSSLSSSSSNsndNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqsnslhpplpanslsk 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 335 ----QKGNLIQHQQGHTGERAYHCGECGKSFRQKFCFINHQRVHTGErPYKCGECGKSFGQKGNLVQHQRGHTGERPYEC 410
Cdd:COG5048  179 dpssNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSA 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 411 KECGKSFRY--RSHLTEHQRLHTGER-----PYNCRECGKLFNRKYHLLVHER--VHTGE--RPYAC--EVCGKLFGNKN 477
Cdd:COG5048  258 SESPRSSLPtaSSQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRND 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 478 CVTIHQRIHTGERPYECNECGKSFLSSSAL-------HVHKRVHSGQKPYKC--SECGKSFAECSSLIKHRRIHTGERPY 548
Cdd:COG5048  338 ALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417
                        410       420
                 ....*....|....*....|....
gi 112983683 549 ECT--KCGKTFQRSSTLLHHQSSH 570
Cdd:COG5048  418 NCKnpPCSKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
394-419 7.57e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.57e-04
                          10        20
                  ....*....|....*....|....*.
gi 112983683  394 NLVQHQRGHTGERPYECKECGKSFRY 419
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
240-423 2.15e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 240 YVCSDCGKSFSRYVSFSNHQR--DHTAKG--PYDCGE--CGKSYSRKSSLIQHQRVHTGKTAYPC--EECGKSFSQKGSL 311
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRsvNHSGESlkPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNN 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 312 ISHQRVHTgerpyecreygksfgQKGNLIQHQQghtgERAYHCgeCGKSFRQKFCFINHQRVHTGERP--YKCGECGKSF 389
Cdd:COG5048  370 EPPQSLQQ---------------YKDLKNDKKS----ETLSNS--CIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428
                        170       180       190
                 ....*....|....*....|....*....|....
gi 112983683 390 GQKGNLVQHQRGHTGERPYECkECGKSFRYRSHL 423
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDL 461
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
408-430 3.88e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 3.88e-03
                          10        20
                  ....*....|....*....|...
gi 112983683  408 YECKECGKSFRYRSHLTEHQRLH 430
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
460-539 4.34e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112983683 460 GERPYACEV--CGKLFGNKNCVTIHqRIHtgerpyecNECGKSFLSSSALHVHKRVHSGQKPYKCSECGKSFAECSSLIK 537
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ..
gi 112983683 538 HR 539
Cdd:COG5189  417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
482-503 5.04e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.04e-03
                          10        20
                  ....*....|....*....|..
gi 112983683  482 HQRIHTGERPYECNECGKSFLS 503
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
534-557 6.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.07e-03
                          10        20
                  ....*....|....*....|....
gi 112983683  534 SLIKHRRIHTGERPYECTKCGKTF 557
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
510-530 8.65e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.65e-03
                          10        20
                  ....*....|....*....|.
gi 112983683  510 HKRVHSGQKPYKCSECGKSFA 530
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-447 8.99e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 112983683  422 HLTEHQRLHTGERPYNCRECGKLFNR 447
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
296-318 9.39e-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: 33.81  E-value: 9.39e-03
                          10        20
                  ....*....|....*....|...
gi 112983683  296 YPCEECGKSFSQKGSLISHQRVH 318
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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