NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530425693|ref|XP_005260759|]
View 

zinc finger protein 337 isoform X2 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016931)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 12-52 2.09e-20

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: 84.44  E-value: 2.09e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530425693   12 LAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSLG 52
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
202-594 9.11e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 9.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 202 KSYVCSVCGRGFSLKANLLRHQRTHSGEKPFLCKVCGRGYTSKSY--LTVHERTHTGEKPYECQECGRRFNDKSSYNKHL 279
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 280 KAHSGEkPFVCKECGRGYTNKSYFVVHK--RIHSGEKPYRCQECGRGF-----SNKSHLI-----------------THQ 335
Cdd:COG5048  112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPGNNSSSvntpqSNSLHPPlpanslskdpssnlsllISS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 336 RTHSGEKPFACRQCKQSFSVKGSLLRHQRTHSGEKPFVCKDCERSFSQKSTLVYHQRTHSGEKPFVCRECGQGFIQKSTL 415
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 416 VKHQITHSEE-------KPFVCKDCGRGFIQKSTFTLHQRT--HSEE--KPYGCRE--CGRRFRDKSSYNKHLRAHLGEK 482
Cdd:COG5048  271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 483 RFFCRDCGRGFTLKPNLTI-------HQRTHSGEKPFMC--KQCEKSFSLKANLLRHQWTHSGERP--FNCKDCGRGFIL 551
Cdd:COG5048  351 PAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNR 430

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 530425693 552 KSTLLFHQKTHSGEKPFICSecgqgfIWKSNLVKHQLAHSGKQ 594
Cdd:COG5048  431 HYNLIPHKKIHTNHAPLLCS------ILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
667-692 5.00e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 530425693  667 DLTVHERIHTGERPYECQECGRKFSN 692
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 ...
 12-52 2.09e-20

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: 84.44  E-value: 2.09e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530425693   12 LAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSLG 52
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
12-52 4.95e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 84.18  E-value: 4.95e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 530425693    12 LAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSLG 52
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-51 7.74e-18

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: 77.20  E-value: 7.74e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530425693  12 LAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSL 51
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
202-594 9.11e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 9.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 202 KSYVCSVCGRGFSLKANLLRHQRTHSGEKPFLCKVCGRGYTSKSY--LTVHERTHTGEKPYECQECGRRFNDKSSYNKHL 279
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 280 KAHSGEkPFVCKECGRGYTNKSYFVVHK--RIHSGEKPYRCQECGRGF-----SNKSHLI-----------------THQ 335
Cdd:COG5048  112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPGNNSSSvntpqSNSLHPPlpanslskdpssnlsllISS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 336 RTHSGEKPFACRQCKQSFSVKGSLLRHQRTHSGEKPFVCKDCERSFSQKSTLVYHQRTHSGEKPFVCRECGQGFIQKSTL 415
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 416 VKHQITHSEE-------KPFVCKDCGRGFIQKSTFTLHQRT--HSEE--KPYGCRE--CGRRFRDKSSYNKHLRAHLGEK 482
Cdd:COG5048  271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 483 RFFCRDCGRGFTLKPNLTI-------HQRTHSGEKPFMC--KQCEKSFSLKANLLRHQWTHSGERP--FNCKDCGRGFIL 551
Cdd:COG5048  351 PAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNR 430

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 530425693 552 KSTLLFHQKTHSGEKPFICSecgqgfIWKSNLVKHQLAHSGKQ 594
Cdd:COG5048  431 HYNLIPHKKIHTNHAPLLCS------ILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
246-270 2.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.09e-03
                          10        20
                  ....*....|....*....|....*
gi 530425693  246 YLTVHERTHTGEKPYECQECGRRFN 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
667-692 5.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 530425693  667 DLTVHERIHTGERPYECQECGRKFSN 692
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 ...
 12-52 2.09e-20

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: 84.44  E-value: 2.09e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530425693   12 LAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSLG 52
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
12-52 4.95e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 84.18  E-value: 4.95e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 530425693    12 LAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSLG 52
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 12-51 7.74e-18

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: 77.20  E-value: 7.74e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530425693  12 LAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSL 51
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
202-594 9.11e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 9.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 202 KSYVCSVCGRGFSLKANLLRHQRTHSGEKPFLCKVCGRGYTSKSY--LTVHERTHTGEKPYECQECGRRFNDKSSYNKHL 279
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 280 KAHSGEkPFVCKECGRGYTNKSYFVVHK--RIHSGEKPYRCQECGRGF-----SNKSHLI-----------------THQ 335
Cdd:COG5048  112 SSSSNS-NDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPGNNSSSvntpqSNSLHPPlpanslskdpssnlsllISS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 336 RTHSGEKPFACRQCKQSFSVKGSLLRHQRTHSGEKPFVCKDCERSFSQKSTLVYHQRTHSGEKPFVCRECGQGFIQKSTL 415
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 416 VKHQITHSEE-------KPFVCKDCGRGFIQKSTFTLHQRT--HSEE--KPYGCRE--CGRRFRDKSSYNKHLRAHLGEK 482
Cdd:COG5048  271 QSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 483 RFFCRDCGRGFTLKPNLTI-------HQRTHSGEKPFMC--KQCEKSFSLKANLLRHQWTHSGERP--FNCKDCGRGFIL 551
Cdd:COG5048  351 PAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNR 430

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 530425693 552 KSTLLFHQKTHSGEKPFICSecgqgfIWKSNLVKHQLAHSGKQ 594
Cdd:COG5048  431 HYNLIPHKKIHTNHAPLLCS------ILKSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
314-706 1.86e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.11  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 314 KPYRCQECGRGFSNKSHLITHQRTHSGEKPFACRQ--CKQSFSVKGSLLRHQRTHSGEKPFVCKDCerSFSQKSTLVYHQ 391
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKS--LPLSNSKASSSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 392 RTHSGEKPFV---CRECGQGFIQKSTLVKHQITHSEEKPFVCKDCGRGFIQ----------------------KSTFTLH 446
Cdd:COG5048  110 LSSSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsnslhpplpanslskdpssNLSLLIS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 447 QRTHSEEKPYGCRECGRRFRDKSSYNKHLRAHLGEKRFFCRDCGRGFTLKPNLTIHQRTHSGEKPFMCKQCEKSFSLKAN 526
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 527 LLRHQWTHSGER-------PFNCKDCGRGFILKSTLLFHQKT--HSGE--KPFICSE--CGQGFIWKSNLVKHQLAHSGK 593
Cdd:COG5048  270 SQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425693 594 QPFVCKECGRGFNWKGNL-------LTHQRTHSGEKPFVCNV-CGQGFSWKRSLTRHHwRIHSKEKPFVCQECKRGYTSK 665
Cdd:COG5048  350 SPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETLSnSCIRNFKRDSNLSLH-IITHLSFRPYNCKNPPCSKSF 428

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 530425693 666 S---DLTVHERIHTGERPYECQECGRKFSnksyySKHLKRHLRE 706
Cdd:COG5048  429 NrhyNLIPHKKIHTNHAPLLCSILKSFRR-----DLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
246-270 2.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.09e-03
                          10        20
                  ....*....|....*....|....*
gi 530425693  246 YLTVHERTHTGEKPYECQECGRRFN 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 316-338 3.53e-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: 35.35  E-value: 3.53e-03
                          10        20
                  ....*....|....*....|...
gi 530425693  316 YRCQECGRGFSNKSHLITHQRTH 338
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
667-692 5.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 5.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 530425693  667 DLTVHERIHTGERPYECQECGRKFSN 692
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH