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Conserved domains on  [gi|257900460|ref|NP_001158187|]
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zinc finger protein 605 isoform 2 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204351)

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;
7-65 3.56e-31

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.77  E-value: 3.56e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460     7 SFEDVAVDFTLEEWQLLNPTQKNLYRDVMLENYSNLVFLGFQILKPDAMFKLEQ-QDPWI 65
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQgEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
199-603 7.79e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 74.35  E-value: 7.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 199 VYLCMECGRFFNKKSQLVIHQRTHTGEKPYQCS--ECGKAFSQKSLLTVHQRTHSGEKPHGCSEC---QKAFSRKSLLIL 273
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplSNSKASSSSLSS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 274 HqrIHTGEKPYGCSECGKAFSRKSQLKR--HQITHTIEKPYS-CSECGKAFSQKLKLITHQRAHtgekpypcSHCGKAFF 350
Cdd:COG5048  113 S--SSNSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLHPPLPAN--------SLSKDPSS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 351 WKSQLITHQRTHTGKKPYGCGECQKaFSRNSLLIRHQRIHTGEKPYECNECGeaFIRKPQLIKHQITHTGEKNY--RCSD 428
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSSDSssSASE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 429 CEEAFFKKSELIRHQKIHLGE-------KPYGCIQCGKTFFGKSQLLTHHRT--HTGE--KPYECSE--CGKAFTQKSSL 495
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDAL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 496 ISHQRTHTGEKPYECSECRKTFSEKSSL-------IHHQRTHTGEKPFEC--SECRKAFAWKPQLLRHQRIHTGEKPYEC 566
Cdd:COG5048  340 KRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNC 419
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 257900460 567 --SECGKAFVQKVQLIKHQRNHTgEKTYGCSDCAKAFFE 603
Cdd:COG5048  420 knPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRR 457
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
620-642 3.43e-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: 3.43e-04
                          10        20
                  ....*....|....*....|...
gi 257900460  620 YKCGECGKSFTRKSHLMRHQRIH 642
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-65 3.56e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.77  E-value: 3.56e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460     7 SFEDVAVDFTLEEWQLLNPTQKNLYRDVMLENYSNLVFLGFQILKPDAMFKLEQ-QDPWI 65
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQgEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
6-46 8.92e-24

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 94.07  E-value: 8.92e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 257900460    6 ISFEDVAVDFTLEEWQLLNPTQKNLYRDVMLENYSNLVFLG 46
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
6-45 3.31e-20

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


Pssm-ID: 143639  Cd Length: 40  Bit Score: 83.75  E-value: 3.31e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 257900460   6 ISFEDVAVDFTLEEWQLLNPTQKNLYRDVMLENYSNLVFL 45
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
199-603 7.79e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 74.35  E-value: 7.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 199 VYLCMECGRFFNKKSQLVIHQRTHTGEKPYQCS--ECGKAFSQKSLLTVHQRTHSGEKPHGCSEC---QKAFSRKSLLIL 273
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplSNSKASSSSLSS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 274 HqrIHTGEKPYGCSECGKAFSRKSQLKR--HQITHTIEKPYS-CSECGKAFSQKLKLITHQRAHtgekpypcSHCGKAFF 350
Cdd:COG5048  113 S--SSNSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLHPPLPAN--------SLSKDPSS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 351 WKSQLITHQRTHTGKKPYGCGECQKaFSRNSLLIRHQRIHTGEKPYECNECGeaFIRKPQLIKHQITHTGEKNY--RCSD 428
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSSDSssSASE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 429 CEEAFFKKSELIRHQKIHLGE-------KPYGCIQCGKTFFGKSQLLTHHRT--HTGE--KPYECSE--CGKAFTQKSSL 495
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDAL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 496 ISHQRTHTGEKPYECSECRKTFSEKSSL-------IHHQRTHTGEKPFEC--SECRKAFAWKPQLLRHQRIHTGEKPYEC 566
Cdd:COG5048  340 KRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNC 419
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 257900460 567 --SECGKAFVQKVQLIKHQRNHTgEKTYGCSDCAKAFFE 603
Cdd:COG5048  420 knPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRR 457
zf-H2C2_2 pfam13465
Zinc-finger double domain;
551-575 1.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|....*
gi 257900460  551 LLRHQRIHTGEKPYECSECGKAFVQ 575
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
620-642 3.43e-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: 3.43e-04
                          10        20
                  ....*....|....*....|...
gi 257900460  620 YKCGECGKSFTRKSHLMRHQRIH 642
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
7-65 3.56e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.77  E-value: 3.56e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460     7 SFEDVAVDFTLEEWQLLNPTQKNLYRDVMLENYSNLVFLGFQILKPDAMFKLEQ-QDPWI 65
Cdd:smart00349   2 TFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQgEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
6-46 8.92e-24

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


Pssm-ID: 460171  Cd Length: 42  Bit Score: 94.07  E-value: 8.92e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 257900460    6 ISFEDVAVDFTLEEWQLLNPTQKNLYRDVMLENYSNLVFLG 46
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
6-45 3.31e-20

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


Pssm-ID: 143639  Cd Length: 40  Bit Score: 83.75  E-value: 3.31e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 257900460   6 ISFEDVAVDFTLEEWQLLNPTQKNLYRDVMLENYSNLVFL 45
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
199-603 7.79e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 74.35  E-value: 7.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 199 VYLCMECGRFFNKKSQLVIHQRTHTGEKPYQCS--ECGKAFSQKSLLTVHQRTHSGEKPHGCSEC---QKAFSRKSLLIL 273
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplSNSKASSSSLSS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 274 HqrIHTGEKPYGCSECGKAFSRKSQLKR--HQITHTIEKPYS-CSECGKAFSQKLKLITHQRAHtgekpypcSHCGKAFF 350
Cdd:COG5048  113 S--SSNSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPgNNSSSVNTPQSNSLHPPLPAN--------SLSKDPSS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 351 WKSQLITHQRTHTGKKPYGCGECQKaFSRNSLLIRHQRIHTGEKPYECNECGeaFIRKPQLIKHQITHTGEKNY--RCSD 428
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSS-SYSIPSSSSDQNLENSSSSLPLTTNS--QLSPKSLLSQSPSSLSSSDSssSASE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 429 CEEAFFKKSELIRHQKIHLGE-------KPYGCIQCGKTFFGKSQLLTHHRT--HTGE--KPYECSE--CGKAFTQKSSL 495
Cdd:COG5048  260 SPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDAL 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 496 ISHQRTHTGEKPYECSECRKTFSEKSSL-------IHHQRTHTGEKPFEC--SECRKAFAWKPQLLRHQRIHTGEKPYEC 566
Cdd:COG5048  340 KRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNC 419
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 257900460 567 --SECGKAFVQKVQLIKHQRNHTgEKTYGCSDCAKAFFE 603
Cdd:COG5048  420 knPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
254-643 6.21e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.18  E-value: 6.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 254 KPHGCSECQKAFSRKSLLILHQRIHTGEKPYGCS--ECGKAFSRKSQLKRHQITHTIEKPYSCSECGKAFSQKLKLITHQ 331
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 332 RAHTGE-KPYPCSHCGKAF--FWKSQLITHQRTHTGKKPY-----GCGECQKAFSRNSLLIRHqrihtgekpyecNECGE 403
Cdd:COG5048  112 SSSSNSnDNNLLSSHSLPPssRDPQLPDLLSISNLRNNPLpgnnsSSVNTPQSNSLHPPLPAN------------SLSKD 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 404 AFIRKPQLIKHQITHTGEKNYRCSDCEEAFFKKSELIRHQKIHLgEKPYGCIQCGKTFFGKSQLLTHHRTHTGEKPYECS 483
Cdd:COG5048  180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSAS 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 484 ECGKAFTQKSSLISHQRTHTGE-------KPYECSECRKTFSEKSSLIHHQRT--HTGE--KPFECSE--CRKAFAWKPQ 550
Cdd:COG5048  259 ESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDA 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 551 LLRHQRIHTGEKPYEC--SECGKAFVQKV------QLIKHQRNHTGEKTYGCSDCAKAFFEKAQLIIHQRIHT---GERP 619
Cdd:COG5048  339 LKRHILLHTSISPAKEklLNSSSKFSPLLnneppqSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHlsfRPYN 418
                        410       420
                 ....*....|....*....|....
gi 257900460 620 YKCGECGKSFTRKSHLMRHQRIHT 643
Cdd:COG5048  419 CKNPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
365-671 9.18e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 9.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 365 KKPYGCGECQKAFSRNSLLIRHQRIHTGEKPYECN--ECGEAFIRKPQLIKHQITHTGEKNYRCSDCE-EAFFKKSELIR 441
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLpLSNSKASSSSL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 442 HQKIHLGEKPYGCIQCGKTFFGKSQLLTHHRTHTGEKPYECSECGKAFTQ----------------------KSSLISHQ 499
Cdd:COG5048  111 SSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsnslhpplpanslskdpssNLSLLISS 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 500 RTHTGEKPYECSECRKTFSEKSSLIHHQRTHTGEKPFECSECRKAFAWKPQLLRHQRIHTGEKPYECSECGKAFVQKVQL 579
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 580 IKHQRNHTGEKT-------YGCSDCAKAFFEKAQLIIHQR--IHTGE--RPYKCGE--CGKSFTRKSHLMRHQRIHTGDK 646
Cdd:COG5048  271 QSSSPNESDSSSekgfslpIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350
                        330       340       350
                 ....*....|....*....|....*....|.
gi 257900460 647 YYGCNECGTT------FNRKSQLMIHQRNHI 671
Cdd:COG5048  351 PAKEKLLNSSskfsplLNNEPPQSLQQYKDL 381
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
226-386 5.55e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 5.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 226 KPYQCSECGKAFSQKSLLTVHQRT--HSGE--KPHGCSE--CQKAFSRKSLLILHQRIHTGEKPYGC--SECGKAFSRKS 297
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 298 QLKRHQITHTI-----EKPYSC--SECGKAFSQKLKLITHQRAHTGEKP--YPCSHCGKAFFWKSQLITHQRTHTGKKPY 368
Cdd:COG5048  368 NNEPPQSLQQYkdlknDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447
                        170
                 ....*....|....*...
gi 257900460 369 GCgECQKAFSRNSLLIRH 386
Cdd:COG5048  448 LC-SILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
174-323 1.15e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 174 CDCSTCRKSSNEEPWLTA--NHITHTGVYL----CME--CGRFFNKKSQLVIHQRTHTGEKPYQC--SECGKAFSQKS-- 241
Cdd:COG5048  290 IKSKQCNISFSRSSPLTRhlRSVNHSGESLkpfsCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnn 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 242 ---LLTVHQRTHSGEKPHGC--SECQKAFSRKSLLILHQRIHTGEKPYGC--SECGKAFSRKSQLKRHQITHTIEKPYSC 314
Cdd:COG5048  370 eppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449

                 ....*....
gi 257900460 315 SECGKAFSQ 323
Cdd:COG5048  450 SILKSFRRD 458
zf-H2C2_2 pfam13465
Zinc-finger double domain;
551-575 1.26e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|....*
gi 257900460  551 LLRHQRIHTGEKPYECSECGKAFVQ 575
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
441-531 2.02e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 44.32  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257900460 441 RHQKIhLGEKPYGC--IQCGKTFfgKSQL-LTHHRTHtgekpyecSECGKAFTQKSSLISHQRTHTGEKPYECSECRKTF 517
Cdd:COG5189  340 RMLKV-KDGKPYKCpvEGCNKKY--KNQNgLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY 408
                         90
                 ....*....|....
gi 257900460 518 SEKSSLIHHqRTHT 531
Cdd:COG5189  409 KNLNGLKYH-RKHS 421
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
620-642 3.43e-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: 3.43e-04
                          10        20
                  ....*....|....*....|...
gi 257900460  620 YKCGECGKSFTRKSHLMRHQRIH 642
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
383-407 6.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.50e-04
                          10        20
                  ....*....|....*....|....*
gi 257900460  383 LIRHQRIHTGEKPYECNECGEAFIR 407
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
215-239 7.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.46e-04
                          10        20
                  ....*....|....*....|....*
gi 257900460  215 LVIHQRTHTGEKPYQCSECGKAFSQ 239
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
467-491 1.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 257900460  467 LLTHHRTHTGEKPYECSECGKAFTQ 491
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
494-518 1.57e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*
gi 257900460  494 SLISHQRTHTGEKPYECSECRKTFS 518
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
228-250 2.12e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|...
gi 257900460  228 YQCSECGKAFSQKSLLTVHQRTH 250
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
299-323 2.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.18e-03
                          10        20
                  ....*....|....*....|....*
gi 257900460  299 LKRHQITHTIEKPYSCSECGKAFSQ 323
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
610-631 2.65e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.65e-03
                          10        20
                  ....*....|....*....|..
gi 257900460  610 HQRIHTGERPYKCGECGKSFTR 631
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
480-502 3.21e-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: 3.21e-03
                          10        20
                  ....*....|....*....|...
gi 257900460  480 YECSECGKAFTQKSSLISHQRTH 502
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
526-546 4.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.00e-03
                          10        20
                  ....*....|....*....|.
gi 257900460  526 HQRTHTGEKPFECSECRKAFA 546
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFK 25
 
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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