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Conserved domains on  [gi|223029512|ref|NP_001138554|]
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zinc finger protein 619 isoform 1 [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;
20-120 2.26e-24

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 96.12  E-value: 2.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512    20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSLyptaggfpldtertekvpgalssflpsssslelilallpm 99
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL---------------------------------------- 40
                           90       100
                   ....*....|....*....|.
gi 223029512   100 sAFPFPKPDLIFQLEQGEAAW 120
Cdd:smart00349  41 -GFQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
256-414 4.73e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 256 HSDFHLHQRVHTN-EKPYTCKECGKTFRYNSKLSRHQ--KIHTGE--KPYSCEE--CGQAFSQNSHLLQHQKLHGGQRPY 328
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 329 ECTDCGKTFSYNSKLI--RHQRIHtgekPFKCKECGKAFSCSYDCII-----------HERIHNGEKPYECK--ECGKSL 393
Cdd:COG5048  353 KEKLLNSSSKFSPLLNnePPQSLQ----QYKDLKNDKKSETLSNSCIrnfkrdsnlslHIITHLSFRPYNCKnpPCSKSF 428
                        170       180
                 ....*....|....*....|.
gi 223029512 394 SSNSVLIQHQRIHTGEKPYEC 414
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-505 8.81e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.81e-05
                          10        20
                  ....*....|....*....|...
gi 223029512  483 LVQHQRVHTGEKPYECKECGKAF 505
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-479 9.11e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.11e-04
                          10        20
                  ....*....|....*....|..
gi 223029512  458 HQRIHNGEKPYECQECGKTFSQ 479
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
20-120 2.26e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 96.12  E-value: 2.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512    20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSLyptaggfpldtertekvpgalssflpsssslelilallpm 99
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL---------------------------------------- 40
                           90       100
                   ....*....|....*....|.
gi 223029512   100 sAFPFPKPDLIFQLEQGEAAW 120
Cdd:smart00349  41 -GFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
19-59 2.46e-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: 2.46e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 223029512   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 5.12e-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: 5.12e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223029512  20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSL 59
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
256-414 4.73e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 256 HSDFHLHQRVHTN-EKPYTCKECGKTFRYNSKLSRHQ--KIHTGE--KPYSCEE--CGQAFSQNSHLLQHQKLHGGQRPY 328
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 329 ECTDCGKTFSYNSKLI--RHQRIHtgekPFKCKECGKAFSCSYDCII-----------HERIHNGEKPYECK--ECGKSL 393
Cdd:COG5048  353 KEKLLNSSSKFSPLLNnePPQSLQ----QYKDLKNDKKSETLSNSCIrnfkrdsnlslHIITHLSFRPYNCKnpPCSKSF 428
                        170       180
                 ....*....|....*....|.
gi 223029512 394 SSNSVLIQHQRIHTGEKPYEC 414
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
343-367 6.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.83e-06
                          10        20
                  ....*....|....*....|....*
gi 223029512  343 LIRHQRIHTGEKPFKCKECGKAFSC 367
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-505 8.81e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.81e-05
                          10        20
                  ....*....|....*....|...
gi 223029512  483 LVQHQRVHTGEKPYECKECGKAF 505
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-479 9.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.11e-04
                          10        20
                  ....*....|....*....|..
gi 223029512  458 HQRIHNGEKPYECQECGKTFSQ 479
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
20-120 2.26e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 96.12  E-value: 2.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512    20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSLyptaggfpldtertekvpgalssflpsssslelilallpm 99
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL---------------------------------------- 40
                           90       100
                   ....*....|....*....|.
gi 223029512   100 sAFPFPKPDLIFQLEQGEAAW 120
Cdd:smart00349  41 -GFQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
19-59 2.46e-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: 2.46e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 223029512   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 5.12e-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: 5.12e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 223029512  20 VTFEDVAVYFTQNEWASLHPTQRALYREVMLENYANVTSL 59
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
256-414 4.73e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 256 HSDFHLHQRVHTN-EKPYTCKECGKTFRYNSKLSRHQ--KIHTGE--KPYSCEE--CGQAFSQNSHLLQHQKLHGGQRPY 328
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 329 ECTDCGKTFSYNSKLI--RHQRIHtgekPFKCKECGKAFSCSYDCII-----------HERIHNGEKPYECK--ECGKSL 393
Cdd:COG5048  353 KEKLLNSSSKFSPLLNnePPQSLQ----QYKDLKNDKKSETLSNSCIrnfkrdsnlslHIITHLSFRPYNCKnpPCSKSF 428
                        170       180
                 ....*....|....*....|.
gi 223029512 394 SSNSVLIQHQRIHTGEKPYEC 414
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
343-367 6.83e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 6.83e-06
                          10        20
                  ....*....|....*....|....*
gi 223029512  343 LIRHQRIHTGEKPFKCKECGKAFSC 367
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
260-525 4.80e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 260 HLHQRVHTNEKPYTC--KECGKTFRYNSKLSRHQKIHTGEKPYSCE-ECGQAFSQNSH--------------LLQHQKLH 322
Cdd:COG5048   50 TRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSsslsssssnsndnnLLSSHSLP 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 323 GGQRPYE-CTDCGKTFSYNSKLIRHQR-----------IHTGEKPFKCKECGKAFSCSydciIHERIHNGEKPYECKECG 390
Cdd:COG5048  130 PSSRDPQlPDLLSISNLRNNPLPGNNSssvntpqsnslHPPLPANSLSKDPSSNLSLL----ISSNVSTSIPSSSENSPL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 391 KSLSSNSVLIQHQRIHTGEKPYECKECGKAFHRSSVFLQHQRFHTGEQLYKCNECWKTFSCSSRFIVHQRIHNGE----- 465
Cdd:COG5048  206 SSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekg 285
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029512 466 --KPYECQECGKTFSQKITLVQHQR--VHTGE--KPYECKE--CGKAFRWNASFIQHQKWHTRKKLIN 525
Cdd:COG5048  286 fsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353
zf-H2C2_2 pfam13465
Zinc-finger double domain;
399-421 5.56e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.56e-05
                          10        20
                  ....*....|....*....|...
gi 223029512  399 LIQHQRIHTGEKPYECKECGKAF 421
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-505 8.81e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.81e-05
                          10        20
                  ....*....|....*....|...
gi 223029512  483 LVQHQRVHTGEKPYECKECGKAF 505
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-479 1.01e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 230 HLITKQGFAKEQVFYKCGECGSYYNPHSDFHLHQRVHTNEKPYTCKECGKTFRYNSKLSRHQKIHTGE-------KPYSC 302
Cdd:COG5048  213 SSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKS 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 303 EECGQAFSQNSHLLQHQ--KLHGGQ--RPYECT--DCGKTFSYNSKLIRHQRIHTGEKPFKCKEcgkafscsydcIIHER 376
Cdd:COG5048  293 KQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKL-----------LNSSS 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 377 IHNGEKPYEckecgkslssNSVLIQHQRIHTGEKPYEC--KECGKAFHRSSVFLQHQRFHTGEQ--LYKCNECWKTFSCS 452
Cdd:COG5048  362 KFSPLLNNE----------PPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRpyNCKNPPCSKSFNRH 431
                        250       260
                 ....*....|....*....|....*..
gi 223029512 453 SRFIVHQRIHNGEKPYECQECGKTFSQ 479
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRRD 458
zf-H2C2_2 pfam13465
Zinc-finger double domain;
287-311 1.32e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.32e-04
                          10        20
                  ....*....|....*....|....*
gi 223029512  287 LSRHQKIHTGEKPYSCEECGQAFSQ 311
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
328-350 2.46e-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: 38.44  E-value: 2.46e-04
                          10        20
                  ....*....|....*....|...
gi 223029512  328 YECTDCGKTFSYNSKLIRHQRIH 350
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
272-294 7.24e-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: 7.24e-04
                          10        20
                  ....*....|....*....|...
gi 223029512  272 YTCKECGKTFRYNSKLSRHQKIH 294
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
458-479 9.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 9.11e-04
                          10        20
                  ....*....|....*....|..
gi 223029512  458 HQRIHNGEKPYECQECGKTFSQ 479
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
298-356 1.05e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029512 298 KPYSCEECGQAFSQNSHLLQHQKLHGGQRPYECTD--CGKTFSYNSKLIRHQRIHTGEKPF 356
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
262-283 1.66e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.66e-03
                          10        20
                  ....*....|....*....|..
gi 223029512  262 HQRVHTNEKPYTCKECGKTFRY 283
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
177-499 2.28e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 177 PDFKDRLEKSQLH-DTGNKTKIGDCTDLTVQDHESSTTEREEIARKLEESSVSTHLITKQGFAKEQVFYKCGECGSYYNP 255
Cdd:COG5048   40 TDSFSRLEHLTRHiRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSND 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 256 HSDFHLHQRVHTNEKPYTCKECGKTFRYNSKLSRHQKIHTGEKPYSC--------EECGQAFSQNSHLLQHQKLHGGQRP 327
Cdd:COG5048  120 NNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSlhpplpanSLSKDPSSNLSLLISSNVSTSIPSS 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 328 YECTDCGKTFSYNSkLIRHQRIHTGEKPFKCKECGKAFSCSYDCIIHERIHNGEKPYECKECGKSLSSNSVLIQHQRIHT 407
Cdd:COG5048  200 SENSPLSSSYSIPS-SSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNES 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 408 GE-------KPYECKECGKAFHRSSVFLQHQR--FHTGEQLykcnecwKTFSCSSRFivhqrihngekpyecqeCGKTFS 478
Cdd:COG5048  279 DSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESL-------KPFSCPYSL-----------------CGKLFS 334
                        330       340
                 ....*....|....*....|.
gi 223029512 479 QKITLVQHQRVHTGEKPYECK 499
Cdd:COG5048  335 RNDALKRHILLHTSISPAKEK 355
zf-H2C2_2 pfam13465
Zinc-finger double domain;
314-339 2.43e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.43e-03
                          10        20
                  ....*....|....*....|....*.
gi 223029512  314 HLLQHQKLHGGQRPYECTDCGKTFSY 339
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
288-365 2.56e-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: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029512 288 SRHQKIhTGEKPYSCE--ECGQAFsQNSHLLQHQKLHGGQRPyectdcgkTFSYNSKLIRHQRIHTGEKPFKCKECGKAF 365
Cdd:COG5189  339 SRMLKV-KDGKPYKCPveGCNKKY-KNQNGLKYHMLHGHQNQ--------KLHENPSPEKMNIFSAKDKPYRCEVCDKRY 408
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
468-490 3.38e-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: 3.38e-03
                          10        20
                  ....*....|....*....|...
gi 223029512  468 YECQECGKTFSQKITLVQHQRVH 490
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
300-322 6.46e-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: 34.58  E-value: 6.46e-03
                          10        20
                  ....*....|....*....|...
gi 223029512  300 YSCEECGQAFSQNSHLLQHQKLH 322
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
374-392 9.44e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.44e-03
                          10
                  ....*....|....*....
gi 223029512  374 HERIHNGEKPYECKECGKS 392
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKS 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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