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Conserved domains on  [gi|400153447|ref|NP_612356|]
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zinc finger protein 551 isoform 1 [Homo sapiens]

Protein Classification

KRAB_A-box and COG5048 domain-containing protein( domain architecture ID 12016953)

protein containing domains KRAB_A-box, COG5048, zf-H2C2_2, and zf-C2H2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 29-69 2.66e-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: 2.66e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 400153447   29 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLG 69
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-624 2.39e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.97  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 279 FECSECEESFSKKCHLILHKIIHTGERPYECSD--REKAFIHKSEFIHHQRRHTGGVRHEC----------------GEC 340
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 341 RKTFSYKSNL---------------IEHQRVHTGERPYE-CGECGKSFRQSSSL-------------------FRHQRVH 385
Cdd:COG5048  114 SSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 386 SGERPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQFSNLIRH 465
Cdd:COG5048  194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 466 RSIHTG-------DRPYECSECEKSFSRKFILIQHQR--VHTGE--RPYECSE--CGKSFTRKSDLIQHRRIHTGTRPYE 532
Cdd:COG5048  274 SPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 533 C--SECGKSFRQRS-----GLIQHRRLHTGERPYEC--SECGKSFSQSASLIQHQRVHTGERPYEC--SECGKSFSQSSS 601
Cdd:COG5048  354 EklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYN 433

                        410       420
                 ....*....|....*....|...
gi 400153447 602 LIQHQRGHTGERPYECSQCGKPF 624
Cdd:COG5048  434 LIPHKKIHTNHAPLLCSILKSFR 456
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 643-665 5.53e-04

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


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 5.53e-04
                          10        20
                  ....*....|....*....|...
gi 400153447  643 YECSECGKSFSRKSNLIRHRRVH 665
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
629-654 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 400153447  629 DLIQHQRVHTGERPYECSECGKSFSR 654
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 29-69 2.66e-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: 2.66e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 400153447   29 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLG 69
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
29-71 2.71e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 87.65  E-value: 2.71e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 400153447    29 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLGYC 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 29-68 1.70e-17

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: 76.05  E-value: 1.70e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 400153447  29 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSL 68
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-624 2.39e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.97  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 279 FECSECEESFSKKCHLILHKIIHTGERPYECSD--REKAFIHKSEFIHHQRRHTGGVRHEC----------------GEC 340
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 341 RKTFSYKSNL---------------IEHQRVHTGERPYE-CGECGKSFRQSSSL-------------------FRHQRVH 385
Cdd:COG5048  114 SSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 386 SGERPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQFSNLIRH 465
Cdd:COG5048  194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 466 RSIHTG-------DRPYECSECEKSFSRKFILIQHQR--VHTGE--RPYECSE--CGKSFTRKSDLIQHRRIHTGTRPYE 532
Cdd:COG5048  274 SPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 533 C--SECGKSFRQRS-----GLIQHRRLHTGERPYEC--SECGKSFSQSASLIQHQRVHTGERPYEC--SECGKSFSQSSS 601
Cdd:COG5048  354 EklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYN 433

                        410       420
                 ....*....|....*....|...
gi 400153447 602 LIQHQRGHTGERPYECSQCGKPF 624
Cdd:COG5048  434 LIPHKKIHTNHAPLLCSILKSFR 456
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 643-665 5.53e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 5.53e-04
                          10        20
                  ....*....|....*....|...
gi 400153447  643 YECSECGKSFSRKSNLIRHRRVH 665
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
573-598 1.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153447  573 SLIQHQRVHTGERPYECSECGKSFSQ 598
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
629-654 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 400153447  629 DLIQHQRVHTGERPYECSECGKSFSR 654
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 558-605 4.71e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 4.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 400153447 558 PYECSECGKSFSQSASLIQHQRVhtGERPYECSECGKSFSQSSSLIQH 605
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDH 118
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 29-69 2.66e-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: 2.66e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 400153447   29 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLG 69
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
29-71 2.71e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 87.65  E-value: 2.71e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 400153447    29 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLGYC 71
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 29-68 1.70e-17

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: 76.05  E-value: 1.70e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 400153447  29 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSL 68
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
279-624 2.39e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.97  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 279 FECSECEESFSKKCHLILHKIIHTGERPYECSD--REKAFIHKSEFIHHQRRHTGGVRHEC----------------GEC 340
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 341 RKTFSYKSNL---------------IEHQRVHTGERPYE-CGECGKSFRQSSSL-------------------FRHQRVH 385
Cdd:COG5048  114 SSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 386 SGERPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQFSNLIRH 465
Cdd:COG5048  194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 466 RSIHTG-------DRPYECSECEKSFSRKFILIQHQR--VHTGE--RPYECSE--CGKSFTRKSDLIQHRRIHTGTRPYE 532
Cdd:COG5048  274 SPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 533 C--SECGKSFRQRS-----GLIQHRRLHTGERPYEC--SECGKSFSQSASLIQHQRVHTGERPYEC--SECGKSFSQSSS 601
Cdd:COG5048  354 EklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYN 433

                        410       420
                 ....*....|....*....|...
gi 400153447 602 LIQHQRGHTGERPYECSQCGKPF 624
Cdd:COG5048  434 LIPHKKIHTNHAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
364-545 5.34e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 5.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 364 ECGECGKSFRQSSSLfRHQRVHSGER-----PYQCCECGKSFRQIFNLIRHRR--VHTGE--MPYQC--SDCGKSFSCKS 432
Cdd:COG5048  259 ESPRSSLPTASSQSS-SPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRND 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 433 ELIQHQRIHSGERPYEC--RECGKSFRQFSN-----LIRHRSIHTGDRPYEC--SECEKSFSRKFILIQHQRVHTGERPY 503
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 400153447 504 EC--SECGKSFTRKSDLIQHRRIHTGTRPYECSECGKSFRQRSG 545
Cdd:COG5048  418 NCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
361-657 5.72e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.10  E-value: 5.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 361 RPYECGECGKSFRQSSSLFRHQRVHSGERPYQC--CECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGK------------ 426
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPlsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 427 ---SFSCKSELIQHQRIHSGERPY--------------ECRECGKSFRQFSNLIRHRSIHTGDRPyecsecEKSFSRKFI 489
Cdd:COG5048  112 sssSNSNDNNLLSSHSLPPSSRDPqlpdllsisnlrnnPLPGNNSSSVNTPQSNSLHPPLPANSL------SKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 490 LIQHQRVHTGERPYECSECGKSFTRKSDLIQHRRIHTGTRPYECSECGKSFRQRSGLIQHRRLHTGERPYECSECGKSFS 569
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 570 QSASLIQHQRVHTGER-------PYECSECGKSFSQSSSLIQHQRG--HTGE--RPYEC--SQCGKPFTHKSDLIQHQRV 636
Cdd:COG5048  266 PTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                        330       340
                 ....*....|....*....|...
gi 400153447 637 HTGERPYEC--SECGKSFSRKSN 657
Cdd:COG5048  346 HTSISPAKEklLNSSSKFSPLLN 368
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
389-666 1.54e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.86  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 389 RPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSD--CGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQF-SNLIRH 465
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKaSSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 466 RSIHTGDRPYECSECEKSFSRKFILIQHQRVHTGERPYECSECGKSFT-----------------------RKSDLIQHR 522
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqsnslhpplpanslskdpssNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 523 RIHTGTRPYECSEcGKSFRQRSGLIQHRRLHTGERPYECSECGKSFSQSASLIQHQRVHTGERPYECSECGKSFSQSSSL 602
Cdd:COG5048  192 VSTSIPSSSENSP-LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 400153447 603 IQHQ------RGHTGER-PYECSQCGKPFTHKSDLIQHQR--VHTGE--RPYECSE--CGKSFSRKSNLIRHRRVHT 666
Cdd:COG5048  271 QSSSpnesdsSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 643-665 5.53e-04

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 5.53e-04
                          10        20
                  ....*....|....*....|...
gi 400153447  643 YECSECGKSFSRKSNLIRHRRVH 665
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
573-598 1.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153447  573 SLIQHQRVHTGERPYECSECGKSFSQ 598
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
629-654 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 400153447  629 DLIQHQRVHTGERPYECSECGKSFSR 654
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
490-514 1.84e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.84e-03
                          10        20
                  ....*....|....*....|....*
gi 400153447  490 LIQHQRVHTGERPYECSECGKSFTR 514
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-458 1.91e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.91e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153447  433 ELIQHQRIHSGERPYECRECGKSFRQ 458
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
405-430 1.91e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.91e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153447  405 NLIRHRRVHTGEMPYQCSDCGKSFSC 430
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 503-525 2.60e-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: 2.60e-03
                          10        20
                  ....*....|....*....|...
gi 400153447  503 YECSECGKSFTRKSDLIQHRRIH 525
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-374 3.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153447  349 NLIEHQRVHTGERPYECGECGKSFRQ 374
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
472-665 3.04e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 472 DRPYECSECEKSFSRKFILIQHQRVHTGERPYECS--ECGKSFTRKSDLIQHRRIHTGTRPYECSECGKSFRQRSGLIQH 549
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 550 RRLHTgERPYECSECGKSFSQSASLIQHQ--RVHTGERPYECSECGKSF--SQSSSLIQHQRGHTgerpyecSQCGKPFT 625
Cdd:COG5048  111 SSSSS-NSNDNNLLSSHSLPPSSRDPQLPdlLSISNLRNNPLPGNNSSSvnTPQSNSLHPPLPAN-------SLSKDPSS 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 400153447 626 HKSDLIQHQRVHTGERPYECSECGKSFSRKSNLIRHRRVH 665
Cdd:COG5048  183 NLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLEN 222
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 363-385 3.14e-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: 3.14e-03
                          10        20
                  ....*....|....*....|...
gi 400153447  363 YECGECGKSFRQSSSLFRHQRVH 385
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
546-570 3.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.62e-03
                          10        20
                  ....*....|....*....|....*
gi 400153447  546 LIQHRRLHTGERPYECSECGKSFSQ 570
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
517-542 3.87e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.87e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153447  517 DLIQHRRIHTGTRPYECSECGKSFRQ 542
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 558-605 4.71e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 4.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 400153447 558 PYECSECGKSFSQSASLIQHQRVhtGERPYECSECGKSFSQSSSLIQH 605
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDH 118
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 471-550 4.72e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.09  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153447 471 GDRPYECS--ECEKSFSRKFILIQHqRVHtgerpyecSECGKSFTRKSDLIQHRRIHTGTRPYECSECGKSFRQRSGLIQ 548
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ..
gi 400153447 549 HR 550
Cdd:COG5189  417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
461-486 6.78e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.78e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153447  461 NLIRHRSIHTGDRPYECSECEKSFSR 486
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 587-609 8.88e-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: 34.20  E-value: 8.88e-03
                          10        20
                  ....*....|....*....|...
gi 400153447  587 YECSECGKSFSQSSSLIQHQRGH 609
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 615-637 9.05e-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: 34.20  E-value: 9.05e-03
                          10        20
                  ....*....|....*....|...
gi 400153447  615 YECSQCGKPFTHKSDLIQHQRVH 637
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 559-581 9.70e-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: 34.20  E-value: 9.70e-03
                          10        20
                  ....*....|....*....|...
gi 400153447  559 YECSECGKSFSQSASLIQHQRVH 581
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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