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Conserved domains on  [gi|1800058300|ref|XP_032004691|]
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LOW QUALITY PROTEIN: zinc finger protein 534-like, partial [Hylobates moloch]

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;
24-84 1.03e-29

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.37  E-value: 1.03e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800058300   24 LSFRDVAIEFSQEEWKCLDPGQKALYKDVMLENYRNLVSLGICLPDLSVISMLEQKRDPWT 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
155-498 5.79e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 155 KPYGCNELGKVFRVSSSLTNHQVIHIADKTYKCS--ECGKIFSSNSNFAQHQRIHTGEKSykYNECGKVFNQNSHLAQHQ 232
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS--DLNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 233 KIHTGEKP-YNNNECEKVFSHHAYLAQHRKIHTREKPYKCSECGKAFSVCSSLTAHLVIHTGEKPHDFKECGKvfrhKSS 311
Cdd:COG5048   110 LSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSS----NLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 312 LTTHQTVHTGERPYKCNECGKGFSRIALLARHQKVHTGEKPYKCNECGKVFIGNSRLARHRKIHTggrRYKCNECGKTFR 391
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS---SDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 392 SCSDLSAH---------LLIHTG-EKPYKCVDCGKVFRHKSSLTYH--CRIHTGE--KPYKCNE--CGKVFSQNSNLQRH 455
Cdd:COG5048   263 SSLPTASSqssspnesdSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1800058300 456 RKIHTGEKLYKC--NECDKVFRQNSH--LAQHRHIHTGEKPYSCNEC 498
Cdd:COG5048   343 ILLHTSISPAKEklLNSSSKFSPLLNnePPQSLQQYKDLKNDKKSET 389
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
24-84 1.03e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.37  E-value: 1.03e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800058300   24 LSFRDVAIEFSQEEWKCLDPGQKALYKDVMLENYRNLVSLGICLPDLSVISMLEQKRDPWT 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 24-64 7.71e-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: 93.69  E-value: 7.71e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1800058300  24 LSFRDVAIEFSQEEWKCLDPGQKALYKDVMLENYRNLVSLG 64
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 24-63 1.90e-20

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: 84.14  E-value: 1.90e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800058300  24 LSFRDVAIEFSQEEWKCLDPGQKALYKDVMLENYRNLVSL 63
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
155-498 5.79e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 155 KPYGCNELGKVFRVSSSLTNHQVIHIADKTYKCS--ECGKIFSSNSNFAQHQRIHTGEKSykYNECGKVFNQNSHLAQHQ 232
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS--DLNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 233 KIHTGEKP-YNNNECEKVFSHHAYLAQHRKIHTREKPYKCSECGKAFSVCSSLTAHLVIHTGEKPHDFKECGKvfrhKSS 311
Cdd:COG5048   110 LSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSS----NLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 312 LTTHQTVHTGERPYKCNECGKGFSRIALLARHQKVHTGEKPYKCNECGKVFIGNSRLARHRKIHTggrRYKCNECGKTFR 391
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS---SDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 392 SCSDLSAH---------LLIHTG-EKPYKCVDCGKVFRHKSSLTYH--CRIHTGE--KPYKCNE--CGKVFSQNSNLQRH 455
Cdd:COG5048   263 SSLPTASSqssspnesdSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1800058300 456 RKIHTGEKLYKC--NECDKVFRQNSH--LAQHRHIHTGEKPYSCNEC 498
Cdd:COG5048   343 ILLHTSISPAKEklLNSSSKFSPLLNnePPQSLQQYKDLKNDKKSET 389
zf-H2C2_2 pfam13465
Zinc-finger double domain;
423-448 2.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.67e-04
                          10        20
                  ....*....|....*....|....*.
gi 1800058300 423 SLTYHCRIHTGEKPYKCNECGKVFSQ 448
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
24-84 1.03e-29

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 110.37  E-value: 1.03e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800058300   24 LSFRDVAIEFSQEEWKCLDPGQKALYKDVMLENYRNLVSLGICLPDLSVISMLEQKRDPWT 84
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 24-64 7.71e-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: 93.69  E-value: 7.71e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1800058300  24 LSFRDVAIEFSQEEWKCLDPGQKALYKDVMLENYRNLVSLG 64
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 24-63 1.90e-20

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: 84.14  E-value: 1.90e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1800058300  24 LSFRDVAIEFSQEEWKCLDPGQKALYKDVMLENYRNLVSL 63
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
155-498 5.79e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 155 KPYGCNELGKVFRVSSSLTNHQVIHIADKTYKCS--ECGKIFSSNSNFAQHQRIHTGEKSykYNECGKVFNQNSHLAQHQ 232
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS--DLNSKSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 233 KIHTGEKP-YNNNECEKVFSHHAYLAQHRKIHTREKPYKCSECGKAFSVCSSLTAHLVIHTGEKPHDFKECGKvfrhKSS 311
Cdd:COG5048   110 LSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSS----NLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 312 LTTHQTVHTGERPYKCNECGKGFSRIALLARHQKVHTGEKPYKCNECGKVFIGNSRLARHRKIHTggrRYKCNECGKTFR 391
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSS---SDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 392 SCSDLSAH---------LLIHTG-EKPYKCVDCGKVFRHKSSLTYH--CRIHTGE--KPYKCNE--CGKVFSQNSNLQRH 455
Cdd:COG5048   263 SSLPTASSqssspnesdSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1800058300 456 RKIHTGEKLYKC--NECDKVFRQNSH--LAQHRHIHTGEKPYSCNEC 498
Cdd:COG5048   343 ILLHTSISPAKEklLNSSSKFSPLLNnePPQSLQQYKDLKNDKKSET 389
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 395-487 5.70e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.48  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800058300 395 DLSAHLLIHTGEKPYKC--VDCGKVFRHKSSLTYHcRIHtgekpykcNECGKVFSQNSNLQRHRKIHTGEKLYKCNECDK 472
Cdd:COG5189   336 DTPSRMLKVKDGKPYKCpvEGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDK 406

                          90
                  ....*....|....*.
gi 1800058300 473 VFRQNSHLAQHR-HIH 487
Cdd:COG5189   407 RYKNLNGLKYHRkHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
423-448 2.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.67e-04
                          10        20
                  ....*....|....*....|....*.
gi 1800058300 423 SLTYHCRIHTGEKPYKCNECGKVFSQ 448
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
451-476 4.54e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 4.54e-04
                          10        20
                  ....*....|....*....|....*.
gi 1800058300 451 NLQRHRKIHTGEKLYKCNECDKVFRQ 476
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 437-459 4.95e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 4.95e-04
                          10        20
                  ....*....|....*....|...
gi 1800058300 437 YKCNECGKVFSQNSNLQRHRKIH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-362 7.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.34e-04
                          10        20
                  ....*....|....*....|...
gi 1800058300 340 LARHQKVHTGEKPYKCNECGKVF 362
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
255-279 1.21e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.21e-03
                          10        20
                  ....*....|....*....|....*
gi 1800058300 255 YLAQHRKIHTREKPYKCSECGKAFS 279
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 185-207 5.80e-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: 5.80e-03
                          10        20
                  ....*....|....*....|...
gi 1800058300 185 YKCSECGKIFSSNSNFAQHQRIH 207
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-392 7.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 7.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 1800058300 367 RLARHRKIHTGGRRYKCNECGKTFRS 392
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
311-336 9.25e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.25e-03
                          10        20
                  ....*....|....*....|....*.
gi 1800058300 311 SLTTHQTVHTGERPYKCNECGKGFSR 336
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 465-487 9.76e-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: 9.76e-03
                          10        20
                  ....*....|....*....|...
gi 1800058300 465 YKCNECDKVFRQNSHLAQHRHIH 487
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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