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Conserved domains on  [gi|282395053|ref|NP_848644|]
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zinc finger protein 678 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016931)

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 pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 43-83 8.00e-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: 88.30  E-value: 8.00e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 282395053   43 LLAFSDVVIEFSPEEWACLDPAQRNLYRDVMFENYRNLVSL 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
138-536 2.59e-17

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 84.75  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 138 CNRLTQCSSTKSKIFQCIECGRNFSWRSILTEHKRIHTGEKPYKC--EECGKVFNRCSNLTKHKRIHTGEKPYKCDECGK 215
Cdd:COG5048   20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 216 VFNWW------------------------SQLTNHKKIHTGEKPYK--CDECDKVFNWWSQLTSHKKIHSgekPYPCEEC 269
Cdd:COG5048  100 LSNSKasssslsssssnsndnnllsshslPPSSRDPQLPDLLSISNlrNNPLPGNNSSSVNTPQSNSLHP---PLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 270 GKAFTQFSNLTQHKRIHTGEKPYKCKECCKAFNKFSNLTQHKRIHTGEKPYKCEECGNVFNEcsHLTRHRRIHTGEKPYK 349
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK--SLLSQSPSSLSSSDSS 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 350 --CEECGKAFTQFASLTRHKRIHTGE-------KPYQCEECGKTFNRCSHLSSHKR--IHTGE--KPYKCEE--CGRTFT 414
Cdd:COG5048  255 ssASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFS 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 415 QFSNLTQHKRIHTGEKPYKCK--ECGKAFNKFS-----SLTQHRRIHTGVKPYKCE--ECGKVFKQCSHLTSHKRIHTGE 485
Cdd:COG5048  335 RNDALKRHILLHTSISPAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSF 414

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282395053 486 KP--YKCKECGKAFYQSSILSKHKRIHTEEKPYKCEECGKaFNQFSSLTRHKR 536
Cdd:COG5048  415 RPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
530-555 1.22e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.22e-03
                          10        20
                  ....*....|....*....|....*.
gi 282395053  530 SLTRHKRIHTGEKRYKCKECGKGFYQ 555
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 ...
 43-83 8.00e-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: 88.30  E-value: 8.00e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 282395053   43 LLAFSDVVIEFSPEEWACLDPAQRNLYRDVMFENYRNLVSL 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
44-101 3.59e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 84.18  E-value: 3.59e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 282395053    44 LAFSDVVIEFSPEEWACLDPAQRNLYRDVMFENYRNLVSLAiLSYSIQDLLPEQDMKD 101
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGE 57
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 44-83 1.01e-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: 76.82  E-value: 1.01e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 282395053  44 LAFSDVVIEFSPEEWACLDPAQRNLYRDVMFENYRNLVSL 83
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
138-536 2.59e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 84.75  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 138 CNRLTQCSSTKSKIFQCIECGRNFSWRSILTEHKRIHTGEKPYKC--EECGKVFNRCSNLTKHKRIHTGEKPYKCDECGK 215
Cdd:COG5048   20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 216 VFNWW------------------------SQLTNHKKIHTGEKPYK--CDECDKVFNWWSQLTSHKKIHSgekPYPCEEC 269
Cdd:COG5048  100 LSNSKasssslsssssnsndnnllsshslPPSSRDPQLPDLLSISNlrNNPLPGNNSSSVNTPQSNSLHP---PLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 270 GKAFTQFSNLTQHKRIHTGEKPYKCKECCKAFNKFSNLTQHKRIHTGEKPYKCEECGNVFNEcsHLTRHRRIHTGEKPYK 349
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK--SLLSQSPSSLSSSDSS 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 350 --CEECGKAFTQFASLTRHKRIHTGE-------KPYQCEECGKTFNRCSHLSSHKR--IHTGE--KPYKCEE--CGRTFT 414
Cdd:COG5048  255 ssASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFS 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 415 QFSNLTQHKRIHTGEKPYKCK--ECGKAFNKFS-----SLTQHRRIHTGVKPYKCE--ECGKVFKQCSHLTSHKRIHTGE 485
Cdd:COG5048  335 RNDALKRHILLHTSISPAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSF 414

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282395053 486 KP--YKCKECGKAFYQSSILSKHKRIHTEEKPYKCEECGKaFNQFSSLTRHKR 536
Cdd:COG5048  415 RPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
334-359 8.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 282395053  334 HLTRHRRIHTGEKPYKCEECGKAFTQ 359
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
530-555 1.22e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.22e-03
                          10        20
                  ....*....|....*....|....*.
gi 282395053  530 SLTRHKRIHTGEKRYKCKECGKGFYQ 555
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 ...
 43-83 8.00e-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: 88.30  E-value: 8.00e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 282395053   43 LLAFSDVVIEFSPEEWACLDPAQRNLYRDVMFENYRNLVSL 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
44-101 3.59e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 84.18  E-value: 3.59e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 282395053    44 LAFSDVVIEFSPEEWACLDPAQRNLYRDVMFENYRNLVSLAiLSYSIQDLLPEQDMKD 101
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGE 57
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 44-83 1.01e-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: 76.82  E-value: 1.01e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 282395053  44 LAFSDVVIEFSPEEWACLDPAQRNLYRDVMFENYRNLVSL 83
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
138-536 2.59e-17

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 84.75  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 138 CNRLTQCSSTKSKIFQCIECGRNFSWRSILTEHKRIHTGEKPYKC--EECGKVFNRCSNLTKHKRIHTGEKPYKCDECGK 215
Cdd:COG5048   20 PKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 216 VFNWW------------------------SQLTNHKKIHTGEKPYK--CDECDKVFNWWSQLTSHKKIHSgekPYPCEEC 269
Cdd:COG5048  100 LSNSKasssslsssssnsndnnllsshslPPSSRDPQLPDLLSISNlrNNPLPGNNSSSVNTPQSNSLHP---PLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 270 GKAFTQFSNLTQHKRIHTGEKPYKCKECCKAFNKFSNLTQHKRIHTGEKPYKCEECGNVFNEcsHLTRHRRIHTGEKPYK 349
Cdd:COG5048  177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPK--SLLSQSPSSLSSSDSS 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 350 --CEECGKAFTQFASLTRHKRIHTGE-------KPYQCEECGKTFNRCSHLSSHKR--IHTGE--KPYKCEE--CGRTFT 414
Cdd:COG5048  255 ssASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFS 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 415 QFSNLTQHKRIHTGEKPYKCK--ECGKAFNKFS-----SLTQHRRIHTGVKPYKCE--ECGKVFKQCSHLTSHKRIHTGE 485
Cdd:COG5048  335 RNDALKRHILLHTSISPAKEKllNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSF 414

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282395053 486 KP--YKCKECGKAFYQSSILSKHKRIHTEEKPYKCEECGKaFNQFSSLTRHKR 536
Cdd:COG5048  415 RPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
262-575 1.30e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 67.03  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 262 KPYPCEECGKAFTQFSNLTQHKRIHTGEKPYKC--KECCKAFNKFSNLTQHKRIHTGEKPYKCEECGNVFNE-CSHLTRH 338
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSkASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 339 RRIHTGEKPYKCEECGKAFTQFASLTRHKRIHTGEKPYQCEEC-GKTFNRCSHLSSHKRIHTGEKPykceecgRTFTQFS 417
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSLS-------KDPSSNL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 418 NLTQHKRIHTGEKPYKCKECGKAFNKFSSLTQHRRIHTGVKPYKCEECG----KVFKQCSHLTSHKRIHTGEKPYKCKEC 493
Cdd:COG5048  185 SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSqlspKSLLSQSPSSLSSSDSSSSASESPRSS 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 494 GKafYQSSILSKHKRIHTEE-----KPYKCEECGKAFNQFSSLTRHKR--IHTGE--KRYKCKE--CGKGFYQSSIHSKY 562
Cdd:COG5048  265 LP--TASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                        330
                 ....*....|...
gi 282395053 563 KRIYTGEEPDKCK 575
Cdd:COG5048  343 ILLHTSISPAKEK 355
zf-H2C2_2 pfam13465
Zinc-finger double domain;
334-359 8.31e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 282395053  334 HLTRHRRIHTGEKPYKCEECGKAFTQ 359
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
418-443 9.53e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 9.53e-05
                          10        20
                  ....*....|....*....|....*.
gi 282395053  418 NLTQHKRIHTGEKPYKCKECGKAFNK 443
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
362-387 1.38e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 282395053  362 SLTRHKRIHTGEKPYQCEECGKTFNR 387
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
278-303 1.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.88e-04
                          10        20
                  ....*....|....*....|....*.
gi 282395053  278 NLTQHKRIHTGEKPYKCKECCKAFNK 303
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
474-499 2.22e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.22e-04
                          10        20
                  ....*....|....*....|....*.
gi 282395053  474 HLTSHKRIHTGEKPYKCKECGKAFYQ 499
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
194-218 2.62e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.62e-04
                          10        20
                  ....*....|....*....|....*
gi 282395053  194 NLTKHKRIHTGEKPYKCDECGKVFN 218
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
390-415 3.62e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.62e-04
                          10        20
                  ....*....|....*....|....*.
gi 282395053  390 HLSSHKRIHTGEKPYKCEECGRTFTQ 415
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
167-191 5.74e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.74e-04
                          10        20
                  ....*....|....*....|....*
gi 282395053  167 LTEHKRIHTGEKPYKCEECGKVFNR 191
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
503-527 6.52e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.52e-04
                          10        20
                  ....*....|....*....|....*
gi 282395053  503 LSKHKRIHTEEKPYKCEECGKAFNQ 527
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
446-471 1.10e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*.
gi 282395053  446 SLTQHRRIHTGVKPYKCEECGKVFKQ 471
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
306-330 1.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|....*
gi 282395053  306 NLTQHKRIHTGEKPYKCEECGNVFN 330
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
530-555 1.22e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.22e-03
                          10        20
                  ....*....|....*....|....*.
gi 282395053  530 SLTRHKRIHTGEKRYKCKECGKGFYQ 555
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 451-535 1.37e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282395053 451 RRIHT-GVKPYKCE--ECGKVFKQCSHLTSHKrihtgekpyKCKECGKAFYQSSILSKHKRIHTEEKPYKCEECGKAFNQ 527
Cdd:COG5189  340 RMLKVkDGKPYKCPveGCNKKYKNQNGLKYHM---------LHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKN 410


                 ....*...
gi 282395053 528 FSSLTRHK 535
Cdd:COG5189  411 LNGLKYHR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
223-246 1.52e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....
gi 282395053  223 LTNHKKIHTGEKPYKCDECDKVFN 246
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
251-275 1.63e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.63e-03
                          10        20
                  ....*....|....*....|....*
gi 282395053  251 LTSHKKIHSGEKPYPCEECGKAFTQ 275
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 180-202 4.11e-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: 4.11e-03
                          10        20
                  ....*....|....*....|...
gi 282395053  180 YKCEECGKVFNRCSNLTKHKRIH 202
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 460-482 7.79e-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: 7.79e-03
                          10        20
                  ....*....|....*....|...
gi 282395053  460 YKCEECGKVFKQCSHLTSHKRIH 482
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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