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Conserved domains on  [gi|2089303101|gb|KAG9467077|]
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hypothetical protein GDO78_015663 [Eleutherodactylus coqui]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 11577727)

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
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
381-812 2.64e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 381 QVDLLPNSSNVTQSTElrSDKLFSCFECGKCFTQKSNLVRHKRTHTGEKPFTC--DKCSKSFTQKSHLVGHQVFHTGEKP 458
Cdd:COG5048    14 SVLSSTPKSTLKSLSN--APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 459 FLCSTCGKCFTHRAILYRHRRVHTGE-RPFICGQCGKSFSYKSYLVEHERFHIKERPYSCSECAKSFAK-KSVLVKHLRV 536
Cdd:COG5048    92 DLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtPQSNSLHPPL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 537 HSEQNPFLCSECEKYFTkksvylkHQRIHTGEKPYLCLECGKCFAKKSVLLDHQRTHTGERPYPCLECGKCFSKKSGLVK 616
Cdd:COG5048   172 PANSLSKDPSSNLSLLI-------SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 617 HHRTHTGEKPFPCPECGKCFSQKSGLVKHQKIHTLE-------KSASCMECETGNTCIHPERHHGFNN-----DERPFLC 684
Cdd:COG5048   245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVnhsgeSLKPFSC 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 685 TE--CGKGFTQKAYLVKHQKIHTGEKPFSC--SECGKRFMLKDHLERHQRIH-----TGEKPFSC--SECGKCFTQKKSL 753
Cdd:COG5048   325 PYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNL 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089303101 754 VEHHKTHTGEKP--FSCSECGKCFTRKCQLEIHHRSHTGEKPFLCSECGKFFIQkSDLVRH 812
Cdd:COG5048   405 SLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD-LDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
668-965 2.59e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 668 HPERHHGFNNDERPFLCTECGKGFTQKAYLVKHQKIHTGEKPFSCS--ECGKRFMLKDHLERHQRIHTGEKPFSCS---- 741
Cdd:COG5048    20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkslp 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 742 ------------ECGKCFTQKKSLVEHHKTHTGEKPFSCSECGKCFTRKCQLE--------------IHHRSHTGEKPFL 795
Cdd:COG5048   100 lsnskasssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPgnnsssvntpqsnsLHPPLPANSLSKD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 796 CSECGKFFIQKS---DLVRHQKSHAGGKLTKNESGEVHRRNDLDERPYLCAECGKCFTQKSYLVKHQKFHTGEKPYSCSE 872
Cdd:COG5048   180 PSSNLSLLISSNvstSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASE 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 873 CGKCFTMKSGLVEHQKIHTGV-------KPFSCPECGKCFTRKSQLEMHQRT--HTGE--KPFSCSE--CGKCFIQRSDL 939
Cdd:COG5048   260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDAL 339
                         330       340
                  ....*....|....*....|....*.
gi 2089303101 940 IRHYRIHTSSTVSKVPSVSVLDAFTI 965
Cdd:COG5048   340 KRHILLHTSISPAKEKLLNSSSKFSP 365
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
91-124 6.44e-08

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: 49.47  E-value: 6.44e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2089303101  91 IRCQDVAVFFSMEEWEYLE-GHKEMYKDVMMADHR 124
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVMLENYE 35
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
381-812 2.64e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 381 QVDLLPNSSNVTQSTElrSDKLFSCFECGKCFTQKSNLVRHKRTHTGEKPFTC--DKCSKSFTQKSHLVGHQVFHTGEKP 458
Cdd:COG5048    14 SVLSSTPKSTLKSLSN--APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 459 FLCSTCGKCFTHRAILYRHRRVHTGE-RPFICGQCGKSFSYKSYLVEHERFHIKERPYSCSECAKSFAK-KSVLVKHLRV 536
Cdd:COG5048    92 DLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtPQSNSLHPPL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 537 HSEQNPFLCSECEKYFTkksvylkHQRIHTGEKPYLCLECGKCFAKKSVLLDHQRTHTGERPYPCLECGKCFSKKSGLVK 616
Cdd:COG5048   172 PANSLSKDPSSNLSLLI-------SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 617 HHRTHTGEKPFPCPECGKCFSQKSGLVKHQKIHTLE-------KSASCMECETGNTCIHPERHHGFNN-----DERPFLC 684
Cdd:COG5048   245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVnhsgeSLKPFSC 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 685 TE--CGKGFTQKAYLVKHQKIHTGEKPFSC--SECGKRFMLKDHLERHQRIH-----TGEKPFSC--SECGKCFTQKKSL 753
Cdd:COG5048   325 PYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNL 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089303101 754 VEHHKTHTGEKP--FSCSECGKCFTRKCQLEIHHRSHTGEKPFLCSECGKFFIQkSDLVRH 812
Cdd:COG5048   405 SLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD-LDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
668-965 2.59e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 668 HPERHHGFNNDERPFLCTECGKGFTQKAYLVKHQKIHTGEKPFSCS--ECGKRFMLKDHLERHQRIHTGEKPFSCS---- 741
Cdd:COG5048    20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkslp 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 742 ------------ECGKCFTQKKSLVEHHKTHTGEKPFSCSECGKCFTRKCQLE--------------IHHRSHTGEKPFL 795
Cdd:COG5048   100 lsnskasssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPgnnsssvntpqsnsLHPPLPANSLSKD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 796 CSECGKFFIQKS---DLVRHQKSHAGGKLTKNESGEVHRRNDLDERPYLCAECGKCFTQKSYLVKHQKFHTGEKPYSCSE 872
Cdd:COG5048   180 PSSNLSLLISSNvstSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASE 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 873 CGKCFTMKSGLVEHQKIHTGV-------KPFSCPECGKCFTRKSQLEMHQRT--HTGE--KPFSCSE--CGKCFIQRSDL 939
Cdd:COG5048   260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDAL 339
                         330       340
                  ....*....|....*....|....*.
gi 2089303101 940 IRHYRIHTSSTVSKVPSVSVLDAFTI 965
Cdd:COG5048   340 KRHILLHTSISPAKEKLLNSSSKFSP 365
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
91-124 6.44e-08

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: 49.47  E-value: 6.44e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2089303101  91 IRCQDVAVFFSMEEWEYLE-GHKEMYKDVMMADHR 124
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVMLENYE 35
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
94-127 5.97e-07

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: 46.70  E-value: 5.97e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2089303101  94 QDVAVFFSMEEWEYL-EGHKEMYKDVMMADHRPLT 127
Cdd:pfam01352   5 EDVAVDFTQEEWALLdPAQRNLYRDVMLENYRNLV 39
KRAB smart00349
krueppel associated box;
95-127 3.05e-06

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 45.28  E-value: 3.05e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2089303101   95 DVAVFFSMEEWEYLE-GHKEMYKDVMMADHRPLT 127
Cdd:smart00349   5 DVAVYFTQEEWEQLDpAQKNLYRDVMLENYSNLV 38
zf-H2C2_2 pfam13465
Zinc-finger double domain;
417-442 6.97e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 6.97e-05
                          10        20
                  ....*....|....*....|....*.
gi 2089303101 417 NLVRHKRTHTGEKPFTCDKCSKSFTQ 442
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
896-918 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: 37.28  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|...
gi 2089303101 896 FSCPECGKCFTRKSQLEMHQRTH 918
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
381-812 2.64e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 381 QVDLLPNSSNVTQSTElrSDKLFSCFECGKCFTQKSNLVRHKRTHTGEKPFTC--DKCSKSFTQKSHLVGHQVFHTGEKP 458
Cdd:COG5048    14 SVLSSTPKSTLKSLSN--APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 459 FLCSTCGKCFTHRAILYRHRRVHTGE-RPFICGQCGKSFSYKSYLVEHERFHIKERPYSCSECAKSFAK-KSVLVKHLRV 536
Cdd:COG5048    92 DLNSKSLPLSNSKASSSSLSSSSSNSnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtPQSNSLHPPL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 537 HSEQNPFLCSECEKYFTkksvylkHQRIHTGEKPYLCLECGKCFAKKSVLLDHQRTHTGERPYPCLECGKCFSKKSGLVK 616
Cdd:COG5048   172 PANSLSKDPSSNLSLLI-------SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 617 HHRTHTGEKPFPCPECGKCFSQKSGLVKHQKIHTLE-------KSASCMECETGNTCIHPERHHGFNN-----DERPFLC 684
Cdd:COG5048   245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSVnhsgeSLKPFSC 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 685 TE--CGKGFTQKAYLVKHQKIHTGEKPFSC--SECGKRFMLKDHLERHQRIH-----TGEKPFSC--SECGKCFTQKKSL 753
Cdd:COG5048   325 PYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNL 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089303101 754 VEHHKTHTGEKP--FSCSECGKCFTRKCQLEIHHRSHTGEKPFLCSECGKFFIQkSDLVRH 812
Cdd:COG5048   405 SLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD-LDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
668-965 2.59e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 668 HPERHHGFNNDERPFLCTECGKGFTQKAYLVKHQKIHTGEKPFSCS--ECGKRFMLKDHLERHQRIHTGEKPFSCS---- 741
Cdd:COG5048    20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkslp 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 742 ------------ECGKCFTQKKSLVEHHKTHTGEKPFSCSECGKCFTRKCQLE--------------IHHRSHTGEKPFL 795
Cdd:COG5048   100 lsnskasssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPgnnsssvntpqsnsLHPPLPANSLSKD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 796 CSECGKFFIQKS---DLVRHQKSHAGGKLTKNESGEVHRRNDLDERPYLCAECGKCFTQKSYLVKHQKFHTGEKPYSCSE 872
Cdd:COG5048   180 PSSNLSLLISSNvstSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASE 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 873 CGKCFTMKSGLVEHQKIHTGV-------KPFSCPECGKCFTRKSQLEMHQRT--HTGE--KPFSCSE--CGKCFIQRSDL 939
Cdd:COG5048   260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDAL 339
                         330       340
                  ....*....|....*....|....*.
gi 2089303101 940 IRHYRIHTSSTVSKVPSVSVLDAFTI 965
Cdd:COG5048   340 KRHILLHTSISPAKEKLLNSSSKFSP 365
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
511-942 7.90e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.57  E-value: 7.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 511 KERPYSCSECAKSFAKKSVLVKHLRVHSEQNPFLCS--ECEKYFTKKSVYLKHQRIHTGEKPYLClecgkcfAKKSVLLD 588
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLN-------SKSLPLSN 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 589 HQRTHTGERpypclECGKCFSKKSGLVKHHRTHTGEKPFPCPECGKCFSQKSGLVKHQKIHTLEKSASC--MECETGNTC 666
Cdd:COG5048   103 SKASSSSLS-----SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSlhPPLPANSLS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 667 IHPERHHGFNNDER---PFLCTECgKGFTQKAYLVKHQKI-HTGEKPFSCSECGKR-FMLKDHLERHQRIHTGEK--PFS 739
Cdd:COG5048   178 KDPSSNLSLLISSNvstSIPSSSE-NSPLSSSYSIPSSSSdQNLENSSSSLPLTTNsQLSPKSLLSQSPSSLSSSdsSSS 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 740 CSECGKCFTQKKSLVEHHKTHTGE-------KPFSCSECGKCFTRKCQLEIH--HRSHTGE--KPFLCSE--CGKFFIQK 806
Cdd:COG5048   257 ASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRN 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 807 SDLVRHQKSHAGGKLTKNESGEvhrrndlderpylcaeCGKCFTQKSYLVKHQKFH-----TGEKPYSC--SECGKCFTM 879
Cdd:COG5048   337 DALKRHILLHTSISPAKEKLLN----------------SSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKR 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089303101 880 KSGLVEHQKIHTGVKP--FSCPECGKCFTRKSQLEMHQRTHTGEKPFSCSECGKcFIQRSDLIRH 942
Cdd:COG5048   401 DSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
91-124 6.44e-08

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: 49.47  E-value: 6.44e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2089303101  91 IRCQDVAVFFSMEEWEYLE-GHKEMYKDVMMADHR 124
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDpAQRDLYRDVMLENYE 35
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
94-127 5.97e-07

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: 46.70  E-value: 5.97e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2089303101  94 QDVAVFFSMEEWEYL-EGHKEMYKDVMMADHRPLT 127
Cdd:pfam01352   5 EDVAVDFTQEEWALLdPAQRNLYRDVMLENYRNLV 39
KRAB smart00349
krueppel associated box;
95-127 3.05e-06

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 45.28  E-value: 3.05e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2089303101   95 DVAVFFSMEEWEYLE-GHKEMYKDVMMADHRPLT 127
Cdd:smart00349   5 DVAVYFTQEEWEQLDpAQKNLYRDVMLENYSNLV 38
zf-H2C2_2 pfam13465
Zinc-finger double domain;
417-442 6.97e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 6.97e-05
                          10        20
                  ....*....|....*....|....*.
gi 2089303101 417 NLVRHKRTHTGEKPFTCDKCSKSFTQ 442
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
724-749 1.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|....*.
gi 2089303101 724 HLERHQRIHTGEKPFSCSECGKCFTQ 749
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
623-702 6.56e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089303101 623 GEKPFPCP--ECGKCFSQKSGLvkhqKIHTLEKSASCMECETGNtcihPERHHGFNNDERPFLCTECGKGFTQKAYLVKH 700
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGL----KYHMLHGHQNQKLHENPS----PEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417

                  ..
gi 2089303101 701 QK 702
Cdd:COG5189   418 RK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
614-638 6.79e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.79e-04
                          10        20
                  ....*....|....*....|....*
gi 2089303101 614 LVKHHRTHTGEKPFPCPECGKCFSQ 638
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
896-918 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: 37.28  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|...
gi 2089303101 896 FSCPECGKCFTRKSQLEMHQRTH 918
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
911-935 1.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|....*
gi 2089303101 911 LEMHQRTHTGEKPFSCSECGKCFIQ 935
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
696-719 2.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.76e-03
                          10        20
                  ....*....|....*....|....
gi 2089303101 696 YLVKHQKIHTGEKPFSCSECGKRF 719
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
883-907 2.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 2.76e-03
                          10        20
                  ....*....|....*....|....*
gi 2089303101 883 LVEHQKIHTGVKPFSCPECGKCFTR 907
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
403-425 3.51e-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: 3.51e-03
                          10        20
                  ....*....|....*....|...
gi 2089303101 403 FSCFECGKCFTQKSNLVRHKRTH 425
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
752-777 5.23e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 5.23e-03
                          10        20
                  ....*....|....*....|....*.
gi 2089303101 752 SLVEHHKTHTGEKPFSCSECGKCFTR 777
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
854-878 5.34e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 5.34e-03
                          10        20
                  ....*....|....*....|....*
gi 2089303101 854 YLVKHQKFHTGEKPYSCSECGKCFT 878
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
627-649 7.48e-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: 7.48e-03
                          10        20
                  ....*....|....*....|...
gi 2089303101 627 FPCPECGKCFSQKSGLVKHQKIH 649
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
924-946 8.25e-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: 8.25e-03
                          10        20
                  ....*....|....*....|...
gi 2089303101 924 FSCSECGKCFIQRSDLIRHYRIH 946
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
586-610 9.72e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.72e-03
                          10        20
                  ....*....|....*....|....*
gi 2089303101 586 LLDHQRTHTGERPYPCLECGKCFSK 610
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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