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Conserved domains on  [gi|400153449|ref|NP_001257867|]
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zinc finger protein 551 isoform 2 [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 ...
 1-41 2.55e-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: 2.55e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 400153449    1 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLG 41
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
251-596 1.46e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 251 FECSECEESFSKKCHLILHKIIHTGERPYECSD--REKAFIHKSEFIHHQRRHTGGVRHEC----------------GEC 312
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 313 RKTFSYKSNL---------------IEHQRVHTGERPYE-CGECGKSFRQSSSL-------------------FRHQRVH 357
Cdd:COG5048  114 SSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 358 SGERPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQFSNLIRH 437
Cdd:COG5048  194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 438 RSIHTG-------DRPYECSECEKSFSRKFILIQHQR--VHTGE--RPYECSE--CGKSFTRKSDLIQHRRIHTGTRPYE 504
Cdd:COG5048  274 SPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 505 C--SECGKSFRQRS-----GLIQHRRLHTGERPYEC--SECGKSFSQSASLIQHQRVHTGERPYEC--SECGKSFSQSSS 573
Cdd:COG5048  354 EklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYN 433

                        410       420
                 ....*....|....*....|...
gi 400153449 574 LIQHQRGHTGERPYECSQCGKPF 596
Cdd:COG5048  434 LIPHKKIHTNHAPLLCSILKSFR 456
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 615-637 7.84e-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: 36.89  E-value: 7.84e-04
                          10        20
                  ....*....|....*....|...
gi 400153449  615 YECSECGKSFSRKSNLIRHRRVH 637
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
601-626 2.12e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  601 DLIQHQRVHTGERPYECSECGKSFSR 626
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 ...
 1-41 2.55e-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: 2.55e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 400153449    1 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLG 41
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
1-43 2.59e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 87.65  E-value: 2.59e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 400153449     1 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLGYC 43
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 1-40 2.00e-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: 2.00e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 400153449   1 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSL 40
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
251-596 1.46e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 251 FECSECEESFSKKCHLILHKIIHTGERPYECSD--REKAFIHKSEFIHHQRRHTGGVRHEC----------------GEC 312
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 313 RKTFSYKSNL---------------IEHQRVHTGERPYE-CGECGKSFRQSSSL-------------------FRHQRVH 357
Cdd:COG5048  114 SSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 358 SGERPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQFSNLIRH 437
Cdd:COG5048  194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 438 RSIHTG-------DRPYECSECEKSFSRKFILIQHQR--VHTGE--RPYECSE--CGKSFTRKSDLIQHRRIHTGTRPYE 504
Cdd:COG5048  274 SPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 505 C--SECGKSFRQRS-----GLIQHRRLHTGERPYEC--SECGKSFSQSASLIQHQRVHTGERPYEC--SECGKSFSQSSS 573
Cdd:COG5048  354 EklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYN 433

                        410       420
                 ....*....|....*....|...
gi 400153449 574 LIQHQRGHTGERPYECSQCGKPF 596
Cdd:COG5048  434 LIPHKKIHTNHAPLLCSILKSFR 456
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 615-637 7.84e-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: 36.89  E-value: 7.84e-04
                          10        20
                  ....*....|....*....|...
gi 400153449  615 YECSECGKSFSRKSNLIRHRRVH 637
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
545-570 1.94e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.94e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  545 SLIQHQRVHTGERPYECSECGKSFSQ 570
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
601-626 2.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  601 DLIQHQRVHTGERPYECSECGKSFSR 626
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 530-577 5.70e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 5.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 400153449 530 PYECSECGKSFSQSASLIQHQRVhtGERPYECSECGKSFSQSSSLIQH 577
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 ...
 1-41 2.55e-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: 2.55e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 400153449    1 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLG 41
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB smart00349
krueppel associated box;
1-43 2.59e-21

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 87.65  E-value: 2.59e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 400153449     1 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSLGYC 43
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 1-40 2.00e-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: 2.00e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 400153449   1 MTFEDVAIYFSQEEWELLDESQRFLYCDVMLENFAHVTSL 40
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
251-596 1.46e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 76.66  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 251 FECSECEESFSKKCHLILHKIIHTGERPYECSD--REKAFIHKSEFIHHQRRHTGGVRHEC----------------GEC 312
Cdd:COG5048   34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplsnskasssslSSS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 313 RKTFSYKSNL---------------IEHQRVHTGERPYE-CGECGKSFRQSSSL-------------------FRHQRVH 357
Cdd:COG5048  114 SSNSNDNNLLsshslppssrdpqlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLhpplpanslskdpssnlslLISSNVS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 358 SGERPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQFSNLIRH 437
Cdd:COG5048  194 TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 438 RSIHTG-------DRPYECSECEKSFSRKFILIQHQR--VHTGE--RPYECSE--CGKSFTRKSDLIQHRRIHTGTRPYE 504
Cdd:COG5048  274 SPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAK 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 505 C--SECGKSFRQRS-----GLIQHRRLHTGERPYEC--SECGKSFSQSASLIQHQRVHTGERPYEC--SECGKSFSQSSS 573
Cdd:COG5048  354 EklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYN 433

                        410       420
                 ....*....|....*....|...
gi 400153449 574 LIQHQRGHTGERPYECSQCGKPF 596
Cdd:COG5048  434 LIPHKKIHTNHAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
336-517 1.81e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.56  E-value: 1.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 336 ECGECGKSFRQSSSLfRHQRVHSGER-----PYQCCECGKSFRQIFNLIRHRR--VHTGE--MPYQC--SDCGKSFSCKS 404
Cdd:COG5048  259 ESPRSSLPTASSQSS-SPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRND 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 405 ELIQHQRIHSGERPYEC--RECGKSFRQFSN-----LIRHRSIHTGDRPYEC--SECEKSFSRKFILIQHQRVHTGERPY 475
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 400153449 476 EC--SECGKSFTRKSDLIQHRRIHTGTRPYECSECGKSFRQRSG 517
Cdd:COG5048  418 NCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
333-629 2.06e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.56  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 333 RPYECGECGKSFRQSSSLFRHQRVHSGERPYQC--CECGKSFRQIFNLIRHRRVHTGEMPYQCSDCGK------------ 398
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPlsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 399 ---SFSCKSELIQHQRIHSGERPY--------------ECRECGKSFRQFSNLIRHRSIHTGDRPyecsecEKSFSRKFI 461
Cdd:COG5048  112 sssSNSNDNNLLSSHSLPPSSRDPqlpdllsisnlrnnPLPGNNSSSVNTPQSNSLHPPLPANSL------SKDPSSNLS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 462 LIQHQRVHTGERPYECSECGKSFTRKSDLIQHRRIHTGTRPYECSECGKSFRQRSGLIQHRRLHTGERPYECSECGKSFS 541
Cdd:COG5048  186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 542 QSASLIQHQRVHTGER-------PYECSECGKSFSQSSSLIQHQRG--HTGE--RPYEC--SQCGKPFTHKSDLIQHQRV 608
Cdd:COG5048  266 PTASSQSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILL 345

                        330       340
                 ....*....|....*....|...
gi 400153449 609 HTGERPYEC--SECGKSFSRKSN 629
Cdd:COG5048  346 HTSISPAKEklLNSSSKFSPLLN 368
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
361-638 5.12e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 5.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 361 RPYQCCECGKSFRQIFNLIRHRRVHTGEMPYQCSD--CGKSFSCKSELIQHQRIHSGERPYECRECGKSFRQF-SNLIRH 437
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKaSSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 438 RSIHTGDRPYECSECEKSFSRKFILIQHQRVHTGERPYECSECGKSFT-----------------------RKSDLIQHR 494
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVntpqsnslhpplpanslskdpssNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 495 RIHTGTRPYECSEcGKSFRQRSGLIQHRRLHTGERPYECSECGKSFSQSASLIQHQRVHTGERPYECSECGKSFSQSSSL 574
Cdd:COG5048  192 VSTSIPSSSENSP-LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 400153449 575 IQHQ------RGHTGER-PYECSQCGKPFTHKSDLIQHQR--VHTGE--RPYECSE--CGKSFSRKSNLIRHRRVHT 638
Cdd:COG5048  271 QSSSpnesdsSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 615-637 7.84e-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: 36.89  E-value: 7.84e-04
                          10        20
                  ....*....|....*....|...
gi 400153449  615 YECSECGKSFSRKSNLIRHRRVH 637
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
545-570 1.94e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.94e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  545 SLIQHQRVHTGERPYECSECGKSFSQ 570
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
601-626 2.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  601 DLIQHQRVHTGERPYECSECGKSFSR 626
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
462-486 2.48e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.48e-03
                          10        20
                  ....*....|....*....|....*
gi 400153449  462 LIQHQRVHTGERPYECSECGKSFTR 486
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
405-430 2.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.58e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  405 ELIQHQRIHSGERPYECRECGKSFRQ 430
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
377-402 2.61e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.61e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  377 NLIRHRRVHTGEMPYQCSDCGKSFSC 402
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 475-497 3.59e-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: 3.59e-03
                          10        20
                  ....*....|....*....|...
gi 400153449  475 YECSECGKSFTRKSDLIQHRRIH 497
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
321-346 4.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.10e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  321 NLIEHQRVHTGERPYECGECGKSFRQ 346
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 335-357 4.41e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.41e-03
                          10        20
                  ....*....|....*....|...
gi 400153449  335 YECGECGKSFRQSSSLFRHQRVH 357
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
518-542 4.89e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.89e-03
                          10        20
                  ....*....|....*....|....*
gi 400153449  518 LIQHRRLHTGERPYECSECGKSFSQ 542
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
444-498 4.96e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 4.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 400153449 444 DRPYECSECEKSFSRKFILIQHQRVHTGERPYECS--ECGKSFTRKSDLIQHRRIHT 498
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 443-522 5.04e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400153449 443 GDRPYECS--ECEKSFSRKFILIQHqRVHtgerpyecSECGKSFTRKSDLIQHRRIHTGTRPYECSECGKSFRQRSGLIQ 520
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ..
gi 400153449 521 HR 522
Cdd:COG5189  417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
489-514 5.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  489 DLIQHRRIHTGTRPYECSECGKSFRQ 514
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 530-577 5.70e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.55  E-value: 5.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 400153449 530 PYECSECGKSFSQSASLIQHQRVhtGERPYECSECGKSFSQSSSLIQH 577
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDH 118
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-458 9.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 400153449  433 NLIRHRSIHTGDRPYECSECEKSFSR 458
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
500-573 9.74e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 9.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 400153449 500 TRPYECSECGKSFRQRSGLIQHRRLHTGERPYECS--ECGKSFSQSASLIQHQRVHTGERPYECSECGKSFSQSSS 573
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKAS 106
 
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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