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Conserved domains on  [gi|223029403|ref|NP_001138565|]
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zinc finger protein 619 isoform 2 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204378)

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;
20-80 5.57e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.92  E-value: 5.57e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029403    20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSLSaFPFPKPDLIFQLEQGEAAW 80
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGEEPW 60
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-327 8.83e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 8.83e-06
                          10        20
                  ....*....|....*....|....*
gi 223029403  303 LIRHQRIHTGEKPFKCKECGKAFSC 327
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
216-374 1.09e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 216 HSDFHLHQRVHTN-EKPYTCKECGKTFRYNSKLSRHQ--KIHTGE--KPYSCEE--CGQAFSQNSHLLQHQKLHGGQRPY 288
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 289 ECTDCGKTFSYNSKLI--RHQRIHtgekPFKCKECGKAFSCSYDCII-----------HERIHNGEKPYECK--ECGKSL 353
Cdd:COG5048  353 KEKLLNSSSKFSPLLNnePPQSLQ----QYKDLKNDKKSETLSNSCIrnfkrdsnlslHIITHLSFRPYNCKnpPCSKSF 428

                        170       180
                 ....*....|....*....|.
gi 223029403 354 SSNSVLIQHQRIHTGEKPYEC 374
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
443-465 1.14e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|...
gi 223029403  443 LVQHQRVHTGEKPYECKECGKAF 465
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
418-439 1.12e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|..
gi 223029403  418 HQRIHNGEKPYECQECGKTFSQ 439
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
20-80 5.57e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.92  E-value: 5.57e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029403    20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSLSaFPFPKPDLIFQLEQGEAAW 80
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 19-59 2.27e-22

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 89.84  E-value: 2.27e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 223029403   19 PVTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSL 59
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 20-59 4.78e-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: 80.29  E-value: 4.78e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223029403  20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSL 59
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-327 8.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 8.83e-06
                          10        20
                  ....*....|....*....|....*
gi 223029403  303 LIRHQRIHTGEKPFKCKECGKAFSC 327
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
216-374 1.09e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 216 HSDFHLHQRVHTN-EKPYTCKECGKTFRYNSKLSRHQ--KIHTGE--KPYSCEE--CGQAFSQNSHLLQHQKLHGGQRPY 288
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 289 ECTDCGKTFSYNSKLI--RHQRIHtgekPFKCKECGKAFSCSYDCII-----------HERIHNGEKPYECK--ECGKSL 353
Cdd:COG5048  353 KEKLLNSSSKFSPLLNnePPQSLQ----QYKDLKNDKKSETLSNSCIrnfkrdsnlslHIITHLSFRPYNCKnpPCSKSF 428

                        170       180
                 ....*....|....*....|.
gi 223029403 354 SSNSVLIQHQRIHTGEKPYEC 374
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-381 7.13e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.13e-05
                          10        20
                  ....*....|....*....|...
gi 223029403  359 LIQHQRIHTGEKPYECKECGKAF 381
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
443-465 1.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|...
gi 223029403  443 LVQHQRVHTGEKPYECKECGKAF 465
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
418-439 1.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|..
gi 223029403  418 HQRIHNGEKPYECQECGKTFSQ 439
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
20-80 5.57e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 111.92  E-value: 5.57e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029403    20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSLSaFPFPKPDLIFQLEQGEAAW 80
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 19-59 2.27e-22

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 89.84  E-value: 2.27e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 223029403   19 PVTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSL 59
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 20-59 4.78e-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: 80.29  E-value: 4.78e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223029403  20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSL 59
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
zf-H2C2_2 pfam13465
Zinc-finger double domain;
303-327 8.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 8.83e-06
                          10        20
                  ....*....|....*....|....*
gi 223029403  303 LIRHQRIHTGEKPFKCKECGKAFSC 327
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
216-374 1.09e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 216 HSDFHLHQRVHTN-EKPYTCKECGKTFRYNSKLSRHQ--KIHTGE--KPYSCEE--CGQAFSQNSHLLQHQKLHGGQRPY 288
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 289 ECTDCGKTFSYNSKLI--RHQRIHtgekPFKCKECGKAFSCSYDCII-----------HERIHNGEKPYECK--ECGKSL 353
Cdd:COG5048  353 KEKLLNSSSKFSPLLNnePPQSLQ----QYKDLKNDKKSETLSNSCIrnfkrdsnlslHIITHLSFRPYNCKnpPCSKSF 428

                        170       180
                 ....*....|....*....|.
gi 223029403 354 SSNSVLIQHQRIHTGEKPYEC 374
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
359-381 7.13e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.13e-05
                          10        20
                  ....*....|....*....|...
gi 223029403  359 LIQHQRIHTGEKPYECKECGKAF 381
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
443-465 1.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|...
gi 223029403  443 LVQHQRVHTGEKPYECKECGKAF 465
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
220-485 1.30e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 220 HLHQRVHTNEKPYTC--KECGKTFRYNSKLSRHQKIHTGEKPYSCE-ECGQAFSQNSH--------------LLQHQKLH 282
Cdd:COG5048   50 TRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSsslsssssnsndnnLLSSHSLP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 283 GGQRPYE-CTDCGKTFSYNSKLIRHQRIHTGEK-------PFKCKECGKAFSCSYDCIIHERIHNGEKPYECKECGKSLS 354
Cdd:COG5048  130 PSSRDPQlPDLLSISNLRNNPLPGNNSSSVNTPqsnslhpPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSY 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 355 SNSVLIQHQRIHTGEKPYECKECGKAFHRSSVFLQHQRFHTGEQLYKCNECWKTFSCSSRFIVHQRIHNGE-------KP 427
Cdd:COG5048  210 SIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLP 289

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029403 428 YECQECGKTFSQKITLVQHQR--VHTGE--KPYECKE--CGKAFRWNASFIQHQKWHTRKKLIN 485
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353
zf-H2C2_2 pfam13465
Zinc-finger double domain;
247-271 1.64e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.64e-04
                          10        20
                  ....*....|....*....|....*
gi 223029403  247 LSRHQKIHTGEKPYSCEECGQAFSQ 271
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
190-439 2.48e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 190 HLITKQGFAKEQVFYKCGECGSYYNPHSDFHLHQRVHTNEKPYTCKECGKTFRYNSKLSRHQKIHTGE-------KPYSC 262
Cdd:COG5048  213 SSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKS 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 263 EECGQAFSQNSHLLQHQ--KLHGGQ--RPYECT--DCGKTFSYNSKLIRHQRIHTGEKPFKCKEcgkafscsydcIIHER 336
Cdd:COG5048  293 KQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKL-----------LNSSS 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 337 IHNGEKPYEckecgkslssNSVLIQHQRIHTGEKPYEC--KECGKAFHRSSVFLQHQRFHTGEQ--LYKCNECWKTFSCS 412
Cdd:COG5048  362 KFSPLLNNE----------PPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRpyNCKNPPCSKSFNRH 431

                        250       260
                 ....*....|....*....|....*..
gi 223029403 413 SRFIVHQRIHNGEKPYECQECGKTFSQ 439
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRRD 458
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 288-310 3.35e-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: 38.05  E-value: 3.35e-04
                          10        20
                  ....*....|....*....|...
gi 223029403  288 YECTDCGKTFSYNSKLIRHQRIH 310
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 232-254 1.00e-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: 36.51  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|...
gi 223029403  232 YTCKECGKTFRYNSKLSRHQKIH 254
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
418-439 1.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|..
gi 223029403  418 HQRIHNGEKPYECQECGKTFSQ 439
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
258-316 1.51e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029403 258 KPYSCEECGQAFSQNSHLLQHQKLHGGQRPYECTD--CGKTFSYNSKLIRHQRIHTGEKPF 316
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
222-243 2.04e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.04e-03
                          10        20
                  ....*....|....*....|..
gi 223029403  222 HQRVHTNEKPYTCKECGKTFRY 243
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 248-325 2.52e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 248 SRHQKIhTGEKPYSCE--ECGQAFsQNSHLLQHQKLHGGQRPyectdcgkTFSYNSKLIRHQRIHTGEKPFKCKECGKAF 325
Cdd:COG5189  339 SRMLKV-KDGKPYKCPveGCNKKY-KNQNGLKYHMLHGHQNQ--------KLHENPSPEKMNIFSAKDKPYRCEVCDKRY 408
zf-H2C2_2 pfam13465
Zinc-finger double domain;
274-299 3.06e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.06e-03
                          10        20
                  ....*....|....*....|....*.
gi 223029403  274 HLLQHQKLHGGQRPYECTDCGKTFSY 299
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 428-450 4.46e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.46e-03
                          10        20
                  ....*....|....*....|...
gi 223029403  428 YECQECGKTFSQKITLVQHQRVH 450
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
137-459 5.08e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 137 PDFKDRLEKSQLH-DTGNKTKIGDCTDLTVQDHESSTTEREEIARKLEESSVSTHLITKQGFAKEQVFYKCGECGSYYNP 215
Cdd:COG5048   40 TDSFSRLEHLTRHiRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSND 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 216 HSDFHLHQRVHTNEKPYTCKECGKTFRYNSKLSRHQKIHTGEKPYSC--------EECGQAFSQNSHLLQHQKLHGGQRP 287
Cdd:COG5048  120 NNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSlhpplpanSLSKDPSSNLSLLISSNVSTSIPSS 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 288 YECTDCGKTFSYNSkLIRHQRIHTGEKPFKCKECGKAFSCSYDCIIHERIHNGEKPYECKECGKSLSSNSVLIQHQRIHT 367
Cdd:COG5048  200 SENSPLSSSYSIPS-SSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNES 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029403 368 GE-------KPYECKECGKAFHRSSVFLQHQR--FHTGEQLykcnecwKTFSCSSRFivhqrihngekpyecqeCGKTFS 438
Cdd:COG5048  279 DSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESL-------KPFSCPYSL-----------------CGKLFS 334

                        330       340
                 ....*....|....*....|.
gi 223029403 439 QKITLVQHQRVHTGEKPYECK 459
Cdd:COG5048  335 RNDALKRHILLHTSISPAKEK 355
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 260-282 8.53e-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: 33.81  E-value: 8.53e-03
                          10        20
                  ....*....|....*....|...
gi 223029403  260 YSCEECGQAFSQNSHLLQHQKLH 282
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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