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Conserved domains on  [gi|223005925|ref|NP_001018857|]
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zinc finger protein 805 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204794)

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 smart00349
krueppel associated box;
13-73 7.66e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.31  E-value: 7.66e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223005925    13 VTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPRPELIYHLEHGQEPWT 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
257-580 1.07e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 257 KPYKCMECGKAFNRKSHLTQHQRIHSGEKPYKCS--ECGKAFTHRSTFVLHNRSHTGEKPFVCKecgKAFRDRPGFIRHY 334
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASSS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 335 IIHSG--ENPYECFECGKVFKHRSYlmwHQQTHTGEKPY-----ECSECGKAFCESAALIHHYVIHTGEkpfecLECGKA 407
Cdd:COG5048  109 SLSSSssNSNDNNLLSSHSLPPSSR---DPQLPDLLSISnlrnnPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 408 FNHRSYLKRHQRIHTGEKPYVCSECGKA--FTHCSTFILHKRAHTGEKPFEC---KECGKAFSNRADLIRHFSIHTGEKP 482
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSysIPSSSSDQNLENSSSSLPLTTNsqlSPKSLLSQSPSSLSSSDSSSSASES 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 483 YECMECGKAFNRRSGLTRHQRIHSG-EKPYECIECGKTFCWSTNLIRH--SIIHTGE--KPYECSE--CGKAFSRSSSLT 555
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALK 340

                        330       340
                 ....*....|....*....|....*
gi 223005925 556 QHQRMHTGRNPISVTDVGRPFTSGQ 580
Cdd:COG5048  341 RHILLHTSISPAKEKLLNSSSKFSP 365
zf-H2C2_2 pfam13465
Zinc-finger double domain;
218-242 3.12e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.12e-04
                          10        20
                  ....*....|....*....|....*
gi 223005925  218 LARHERIHSGVKPYECTECGKTFSK 242
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
13-73 7.66e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.31  E-value: 7.66e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223005925    13 VTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPRPELIYHLEHGQEPWT 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-53 3.34e-23

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: 92.53  E-value: 3.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 223005925   12 SVTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSLG 53
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 13-52 1.60e-19

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 81.83  E-value: 1.60e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223005925  13 VTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSL 52
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
257-580 1.07e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 257 KPYKCMECGKAFNRKSHLTQHQRIHSGEKPYKCS--ECGKAFTHRSTFVLHNRSHTGEKPFVCKecgKAFRDRPGFIRHY 334
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASSS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 335 IIHSG--ENPYECFECGKVFKHRSYlmwHQQTHTGEKPY-----ECSECGKAFCESAALIHHYVIHTGEkpfecLECGKA 407
Cdd:COG5048  109 SLSSSssNSNDNNLLSSHSLPPSSR---DPQLPDLLSISnlrnnPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 408 FNHRSYLKRHQRIHTGEKPYVCSECGKA--FTHCSTFILHKRAHTGEKPFEC---KECGKAFSNRADLIRHFSIHTGEKP 482
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSysIPSSSSDQNLENSSSSLPLTTNsqlSPKSLLSQSPSSLSSSDSSSSASES 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 483 YECMECGKAFNRRSGLTRHQRIHSG-EKPYECIECGKTFCWSTNLIRH--SIIHTGE--KPYECSE--CGKAFSRSSSLT 555
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALK 340

                        330       340
                 ....*....|....*....|....*
gi 223005925 556 QHQRMHTGRNPISVTDVGRPFTSGQ 580
Cdd:COG5048  341 RHILLHTSISPAKEKLLNSSSKFSP 365
zf-H2C2_2 pfam13465
Zinc-finger double domain;
413-438 7.66e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 7.66e-06
                          10        20
                  ....*....|....*....|....*.
gi 223005925  413 YLKRHQRIHTGEKPYVCSECGKAFTH 438
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
218-242 3.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.12e-04
                          10        20
                  ....*....|....*....|....*
gi 223005925  218 LARHERIHSGVKPYECTECGKTFSK 242
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
13-73 7.66e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.31  E-value: 7.66e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223005925    13 VTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPRPELIYHLEHGQEPWT 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-53 3.34e-23

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: 92.53  E-value: 3.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 223005925   12 SVTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSLG 53
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 13-52 1.60e-19

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 81.83  E-value: 1.60e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223005925  13 VTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSL 52
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
257-580 1.07e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.49  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 257 KPYKCMECGKAFNRKSHLTQHQRIHSGEKPYKCS--ECGKAFTHRSTFVLHNRSHTGEKPFVCKecgKAFRDRPGFIRHY 334
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS---KSLPLSNSKASSS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 335 IIHSG--ENPYECFECGKVFKHRSYlmwHQQTHTGEKPY-----ECSECGKAFCESAALIHHYVIHTGEkpfecLECGKA 407
Cdd:COG5048  109 SLSSSssNSNDNNLLSSHSLPPSSR---DPQLPDLLSISnlrnnPLPGNNSSSVNTPQSNSLHPPLPAN-----SLSKDP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 408 FNHRSYLKRHQRIHTGEKPYVCSECGKA--FTHCSTFILHKRAHTGEKPFEC---KECGKAFSNRADLIRHFSIHTGEKP 482
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSysIPSSSSDQNLENSSSSLPLTTNsqlSPKSLLSQSPSSLSSSDSSSSASES 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 483 YECMECGKAFNRRSGLTRHQRIHSG-EKPYECIECGKTFCWSTNLIRH--SIIHTGE--KPYECSE--CGKAFSRSSSLT 555
Cdd:COG5048  261 PRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALK 340

                        330       340
                 ....*....|....*....|....*
gi 223005925 556 QHQRMHTGRNPISVTDVGRPFTSGQ 580
Cdd:COG5048  341 RHILLHTSISPAKEKLLNSSSKFSP 365
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
192-568 4.63e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 4.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 192 KNPVIQEEENIFKCNECEKVFNKKRLLARHERIHSGVKPYECTECGKTFSKSTY--LLQHHMVHTGEKPYkcMECGKAFN 269
Cdd:COG5048   23 TLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSD--LNSKSLPL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 270 RKSHLTQHQRIHSGE---KPYKCSECGKAFTHRSTFVLHNRSHTGEKPFVCKECGKAFRDRPGFIRHYIIHSGENPyecf 346
Cdd:COG5048  101 SNSKASSSSLSSSSSnsnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSL---- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 347 eCGKVFKHRSYLMWHQQTHTGEKPYECSECGKA----FCESAALIHHYVIH--------------------TGEKPFECL 402
Cdd:COG5048  177 -SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSysipSSSSDQNLENSSSSlplttnsqlspksllsqspsSLSSSDSSS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 403 ECGKAFNHRSYLKRHQRIH----------TGEKPYVCSECGKAFTHCSTFILHKRA--HTGE--KPFECKE--CGKAFSN 466
Cdd:COG5048  256 SASESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSR 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 467 RADLIRHFSIHTGEKPYECMEC-------GKAFNRRSGLTRHQRIHSGEKPYECI--ECGKTFCWSTNLIRHSIIHTGEK 537
Cdd:COG5048  336 NDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFR 415

                        410       420       430
                 ....*....|....*....|....*....|...
gi 223005925 538 PYEC--SECGKAFSRSSSLTQHQRMHTGRNPIS 568
Cdd:COG5048  416 PYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLL 448
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
229-448 7.51e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 7.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 229 KPYECTECGKTFSKSTYLLQH--HMVHTGE--KPYKCME--CGKAFNRKSHLTQHQRIHSGEKPYKCSECGkafthrstf 302
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLN--------- 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005925 303 vlHNRSHTGEKPfvckecgkafRDRPGFIRHYIIHSGENPYEC--FECGKVFKHRSYLMWHQQTHTGEKPYECSecgkaf 380
Cdd:COG5048  359 --SSSKFSPLLN----------NEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCK------ 420

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223005925 381 cesaalihhyvihtgekpfeCLECGKAFNHRSYLKRHQRIHTgEKPYVCSECGKAFTHCSTFILHKRA 448
Cdd:COG5048  421 --------------------NPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
413-438 7.66e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 7.66e-06
                          10        20
                  ....*....|....*....|....*.
gi 223005925  413 YLKRHQRIHTGEKPYVCSECGKAFTH 438
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
273-298 3.53e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.53e-05
                          10        20
                  ....*....|....*....|....*.
gi 223005925  273 HLTQHQRIHSGEKPYKCSECGKAFTH 298
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
525-550 7.67e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.67e-05
                          10        20
                  ....*....|....*....|....*.
gi 223005925  525 NLIRHSIIHTGEKPYECSECGKAFSR 550
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
357-380 1.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.25e-04
                          10        20
                  ....*....|....*....|....
gi 223005925  357 YLMWHQQTHTGEKPYECSECGKAF 380
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
498-520 1.84e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.84e-04
                          10        20
                  ....*....|....*....|...
gi 223005925  498 LTRHQRIHSGEKPYECIECGKTF 520
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
469-494 2.97e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.97e-04
                          10        20
                  ....*....|....*....|....*.
gi 223005925  469 DLIRHFSIHTGEKPYECMECGKAFNR 494
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
218-242 3.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.12e-04
                          10        20
                  ....*....|....*....|....*
gi 223005925  218 LARHERIHSGVKPYECTECGKTFSK 242
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 539-561 5.33e-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: 37.66  E-value: 5.33e-04
                          10        20
                  ....*....|....*....|...
gi 223005925  539 YECSECGKAFSRSSSLTQHQRMH 561
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 259-281 5.88e-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: 5.88e-04
                          10        20
                  ....*....|....*....|...
gi 223005925  259 YKCMECGKAFNRKSHLTQHQRIH 281
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
245-270 6.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.77e-04
                          10        20
                  ....*....|....*....|....*.
gi 223005925  245 YLLQHHMVHTGEKPYKCMECGKAFNR 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 399-421 1.73e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.73e-03
                          10        20
                  ....*....|....*....|...
gi 223005925  399 FECLECGKAFNHRSYLKRHQRIH 421
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 483-505 2.56e-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: 2.56e-03
                          10        20
                  ....*....|....*....|...
gi 223005925  483 YECMECGKAFNRRSGLTRHQRIH 505
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 343-365 3.12e-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: 3.12e-03
                          10        20
                  ....*....|....*....|...
gi 223005925  343 YECFECGKVFKHRSYLMWHQQTH 365
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-466 4.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.12e-03
                          10        20
                  ....*....|....*....|..
gi 223005925  445 HKRAHTGEKPFECKECGKAFSN 466
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
305-324 4.46e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.46e-03
                          10        20
                  ....*....|....*....|
gi 223005925  305 HNRSHTGEKPFVCKECGKAF 324
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSF 24
 
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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