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Conserved domains on  [gi|27819592|ref|NP_081753|]
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zinc finger protein 398 isoform 1 [Mus musculus]

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;
143-203 3.00e-17

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 76.09  E-value: 3.00e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27819592    143 VAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLISMDYAMNQPDVLSQIQPEGEHST 203
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
368-588 1.59e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 368 EHPLTCAQCPKHFTPQADVGSTSQDHANE-------TPPTCPHCARTFTHPSRLTYHLRVHNSTE---RPFLCP--DCPK 435
Cdd:COG5048 252 DSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVNHSGeslKPFSCPysLCGK 331

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 436 RFADQARLTSHRRAHATERPFRCPQCGRSFslKISLLLHQRGHAQerpfSCPQCGIDFNghsalirhqmiHTGERPYPCt 515
Cdd:COG5048 332 LFSRNDALKRHILLHTSISPAKEKLLNSSS--KFSPLLNNEPPQS----LQQYKDLKND-----------KKSETLSNS- 393

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27819592 516 dCSKSFMRKEHLLNHRRLHTGERP--FQCPHCGKSFIRKHHLMKHQRIHTGERPYPCAVCgRSFRYKQTLKDHLR 588
Cdd:COG5048 394 -CIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGK 466
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
143-203 3.00e-17

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 76.09  E-value: 3.00e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27819592    143 VAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLISMDYAMNQPDVLSQIQPEGEHST 203
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 143-182 3.97e-17

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: 74.89  E-value: 3.97e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27819592 143 VAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLISM 182
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 142-183 5.25e-14

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: 66.34  E-value: 5.25e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 27819592   142 PVAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLISMD 183
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
368-588 1.59e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 368 EHPLTCAQCPKHFTPQADVGSTSQDHANE-------TPPTCPHCARTFTHPSRLTYHLRVHNSTE---RPFLCP--DCPK 435
Cdd:COG5048 252 DSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVNHSGeslKPFSCPysLCGK 331

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 436 RFADQARLTSHRRAHATERPFRCPQCGRSFslKISLLLHQRGHAQerpfSCPQCGIDFNghsalirhqmiHTGERPYPCt 515
Cdd:COG5048 332 LFSRNDALKRHILLHTSISPAKEKLLNSSS--KFSPLLNNEPPQS----LQQYKDLKND-----------KKSETLSNS- 393

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27819592 516 dCSKSFMRKEHLLNHRRLHTGERP--FQCPHCGKSFIRKHHLMKHQRIHTGERPYPCAVCgRSFRYKQTLKDHLR 588
Cdd:COG5048 394 -CIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGK 466
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 540-562 3.19e-06

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: 43.83  E-value: 3.19e-06
                          10        20
                  ....*....|....*....|...
gi 27819592   540 FQCPHCGKSFIRKHHLMKHQRIH 562
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
540-562 3.61e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 3.61e-03
                           10        20
                   ....*....|....*....|...
gi 27819592    540 FQCPHCGKSFIRKHHLMKHQRIH 562
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
143-203 3.00e-17

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 76.09  E-value: 3.00e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27819592    143 VAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLISMDYAMNQPDVLSQIQPEGEHST 203
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 143-182 3.97e-17

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: 74.89  E-value: 3.97e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27819592 143 VAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLISM 182
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 142-183 5.25e-14

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: 66.34  E-value: 5.25e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 27819592   142 PVAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLISMD 183
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
368-588 1.59e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 368 EHPLTCAQCPKHFTPQADVGSTSQDHANE-------TPPTCPHCARTFTHPSRLTYHLRVHNSTE---RPFLCP--DCPK 435
Cdd:COG5048 252 DSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVNHSGeslKPFSCPysLCGK 331

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 436 RFADQARLTSHRRAHATERPFRCPQCGRSFslKISLLLHQRGHAQerpfSCPQCGIDFNghsalirhqmiHTGERPYPCt 515
Cdd:COG5048 332 LFSRNDALKRHILLHTSISPAKEKLLNSSS--KFSPLLNNEPPQS----LQQYKDLKND-----------KKSETLSNS- 393

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27819592 516 dCSKSFMRKEHLLNHRRLHTGERP--FQCPHCGKSFIRKHHLMKHQRIHTGERPYPCAVCgRSFRYKQTLKDHLR 588
Cdd:COG5048 394 -CIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
347-570 4.38e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 4.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 347 HHCGKSLSQDMLMTHQCGHAAEHPLTCAQCPK-HFTPQADVGSTS----QDHANETPPTCPHCARTFTHPSRLTYHLRVH 421
Cdd:COG5048 112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSIsNLRNNPLPGNNSssvnTPQSNSLHPPLPANSLSKDPSSNLSLLISSN 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 422 NSTERPFLCPDCPKRFA--DQARLTSHRRAHATERPFrCPQCGRSFSLKISLLLHQRGHAQERPFSCPQCGIDFNGHSAL 499
Cdd:COG5048 192 VSTSIPSSSENSPLSSSysIPSSSSDQNLENSSSSLP-LTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 500 IRHQMIHTGER-------PYPCTDCSKSFMRKEHLLNHRR--LHTGE--RPFQCPH--CGKSFIRKHHLMKHQRIHTGER 566
Cdd:COG5048 271 QSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350


                ....
gi 27819592 567 PYPC 570
Cdd:COG5048 351 PAKE 354
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 540-562 3.19e-06

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: 43.83  E-value: 3.19e-06
                          10        20
                  ....*....|....*....|...
gi 27819592   540 FQCPHCGKSFIRKHHLMKHQRIH 562
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
554-579 1.04e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.04e-05
                          10        20
                  ....*....|....*....|....*.
gi 27819592   554 HLMKHQRIHTGERPYPCAVCGRSFRY 579
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-551 2.05e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 2.05e-05
                          10        20
                  ....*....|....*....|....*.
gi 27819592   526 HLLNHRRLHTGERPFQCPHCGKSFIR 551
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
510-563 2.54e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.54e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27819592 510 RPYPCTDCSKSFMRKEHLLNHRRLHTGERPFQCPH--CGKSFIRKHHLMKHQRIHT 563
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHH 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
411-562 3.30e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 3.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 411 PSRLTYHLRVHNSTERPFLCPDCpkrfADQARLTSHRRAHATERPFRCPQCGRSFSLKISLLLHQRGH---------AQE 481
Cdd:COG5048 212 PSSSSDQNLENSSSSLPLTTNSQ----LSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPnesdsssekGFS 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27819592 482 RPFSCPQCGIDFNGHSALIRHQ--MIHTGE--RPYPCT--DCSKSFMRKEHLLNHRRLHTGERPFQCP--HCGKSFIRKH 553
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLL 367


                ....*....
gi 27819592 554 HLMKHQRIH 562
Cdd:COG5048 368 NNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
454-520 6.71e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 6.71e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27819592 454 RPFRCPQCGRSFSLKISLLLHQRGHAQERPFSCPQCGID--FNGHSALIRHQMIHTGERPYPCTDCSKS 520
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNSKSLPL 100
zf-H2C2_2 pfam13465
Zinc-finger double domain;
498-521 1.19e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.19e-04
                          10        20
                  ....*....|....*....|....
gi 27819592   498 ALIRHQMIHTGERPYPCTDCSKSF 521
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 512-534 2.43e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.43e-03
                          10        20
                  ....*....|....*....|...
gi 27819592   512 YPCTDCSKSFMRKEHLLNHRRLH 534
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
540-562 3.61e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 3.61e-03
                           10        20
                   ....*....|....*....|...
gi 27819592    540 FQCPHCGKSFIRKHHLMKHQRIH 562
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
480-548 4.93e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 4.93e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27819592 480 QERPFSCPQCGIDFNGHSALIRHQMIHTGERPYPCTD--CSKSFMRKEHLLNHRRLHTGERPFQCPHCGKS 548
Cdd:COG5048  30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL 100
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 540-562 6.28e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.54  E-value: 6.28e-03
                          10        20
                  ....*....|....*....|...
gi 27819592   540 FQCPHCGKSFIRKHHLMKHQRIH 562
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 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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