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Conserved domains on  [gi|528993760|ref|XP_005219868|]
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zinc finger protein 543 isoform X2 [Bos taurus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0003677|GO:0008270|GO:0005515|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|8183940|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-65 2.74e-26

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 100.74  E-value: 2.74e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528993760     8 VTYEDVAVTFTQEEWGHLGPMQRTLYWEVMLETCRLLVSLGCPLPEPDLISPVEPGPE 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
236-442 9.58e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 236 SKSTHLLQHHLIPTREKPYECSECGKAFHRRSQLTTHQLIHTG-EKPYECSECGKGFCDSTRLIKH--SIIHTGE--KPY 310
Cdd:COG5048  243 QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 311 NCLE--CGKAFYRKSYLKEHQRIHTGEKPYVCTECGR------AFVYCS--TFILHKRAHTGEKPYGC-KECGKAFSSRS 379
Cdd:COG5048  323 SCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfspLLNNEPpqSLQQYKDLKNDKKSETLsNSCIRNFKRDS 402

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528993760 380 SLSRHFTIHSAEKP--YKCTECGKAFNRRAYLSSHQRIHSgEKPYTCVECRKTFWWSSSLVRHSI 442
Cdd:COG5048  403 NLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 52-175 1.61e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760   52 PEPDLISPVEPGPESQTSGSGPTPSSCSGDNTKPETPQPAPSHPAPSEEVSPQKRPSQRASGHSQLEQTKDADRPLEMRE 131
Cdd:PHA03307  802 LRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRA 881

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528993760  132 GPL-------RPGTGPQGKELPGKVNPDHHGLGTDDC--LPSRTAQQRVPPGD 175
Cdd:PHA03307  882 RPGaaappkaAAAAPPAGAPAPRPRPAPRVKLGPMPPggPDPRGGFRRVPPGD 934
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-65 2.74e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 100.74  E-value: 2.74e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528993760     8 VTYEDVAVTFTQEEWGHLGPMQRTLYWEVMLETCRLLVSLGCPLPEPDLISPVEPGPE 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 1.56e-21

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: 87.14  E-value: 1.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 528993760    7 PVTYEDVAVTFTQEEWGHLGPMQRTLYWEVMLETCRLLVSLG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-47 6.10e-18

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: 6.10e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 528993760   8 VTYEDVAVTFTQEEWGHLGPMQRTLYWEVMLETCRLLVSL 47
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
236-442 9.58e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 236 SKSTHLLQHHLIPTREKPYECSECGKAFHRRSQLTTHQLIHTG-EKPYECSECGKGFCDSTRLIKH--SIIHTGE--KPY 310
Cdd:COG5048  243 QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 311 NCLE--CGKAFYRKSYLKEHQRIHTGEKPYVCTECGR------AFVYCS--TFILHKRAHTGEKPYGC-KECGKAFSSRS 379
Cdd:COG5048  323 SCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfspLLNNEPpqSLQQYKDLKNDKKSETLsNSCIRNFKRDS 402

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528993760 380 SLSRHFTIHSAEKP--YKCTECGKAFNRRAYLSSHQRIHSgEKPYTCVECRKTFWWSSSLVRHSI 442
Cdd:COG5048  403 NLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
324-349 3.67e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.67e-05
                          10        20
                  ....*....|....*....|....*.
gi 528993760  324 YLKEHQRIHTGEKPYVCTECGRAFVY 349
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 52-175 1.61e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760   52 PEPDLISPVEPGPESQTSGSGPTPSSCSGDNTKPETPQPAPSHPAPSEEVSPQKRPSQRASGHSQLEQTKDADRPLEMRE 131
Cdd:PHA03307  802 LRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRA 881

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528993760  132 GPL-------RPGTGPQGKELPGKVNPDHHGLGTDDC--LPSRTAQQRVPPGD 175
Cdd:PHA03307  882 RPGaaappkaAAAAPPAGAPAPRPRPAPRVKLGPMPPggPDPRGGFRRVPPGD 934
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 50-136 8.97e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 38.59  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760   50 PLPEPDLISPVEPGPESQTSGSGPTPsscsgdntKPETPQPAPSHPAPSEEVSPQKrPSQRASGHSQLEQTKDADRPLEM 129
Cdd:pfam03154 265 PLPQPSLHGQMPPMPHSLQTGPSHMQ--------HPVPPQPFPLTPQSSQSQVPPG-PSPAAPGQSQQRIHTPPSQSQLQ 335

                          90
                  ....*....|..
gi 528993760  130 -----REGPLRP 136
Cdd:pfam03154 336 sqqppREQPLPP 347
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-65 2.74e-26

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 100.74  E-value: 2.74e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528993760     8 VTYEDVAVTFTQEEWGHLGPMQRTLYWEVMLETCRLLVSLGCPLPEPDLISPVEPGPE 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 1.56e-21

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: 87.14  E-value: 1.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 528993760    7 PVTYEDVAVTFTQEEWGHLGPMQRTLYWEVMLETCRLLVSLG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-47 6.10e-18

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: 6.10e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 528993760   8 VTYEDVAVTFTQEEWGHLGPMQRTLYWEVMLETCRLLVSL 47
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
236-442 9.58e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 236 SKSTHLLQHHLIPTREKPYECSECGKAFHRRSQLTTHQLIHTG-EKPYECSECGKGFCDSTRLIKH--SIIHTGE--KPY 310
Cdd:COG5048  243 QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 311 NCLE--CGKAFYRKSYLKEHQRIHTGEKPYVCTECGR------AFVYCS--TFILHKRAHTGEKPYGC-KECGKAFSSRS 379
Cdd:COG5048  323 SCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfspLLNNEPpqSLQQYKDLKNDKKSETLsNSCIRNFKRDS 402

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528993760 380 SLSRHFTIHSAEKP--YKCTECGKAFNRRAYLSSHQRIHSgEKPYTCVECRKTFWWSSSLVRHSI 442
Cdd:COG5048  403 NLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
71-359 6.55e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760  71 SGPTPSSCSGDNTKPETPQPAPSHPAPSEevsPQKRPSQRASGHSQLEQTKDADRPLeMREGPLRPGTGPQGKELpGKVN 150
Cdd:COG5048  176 LSKDPSSNLSLLISSNVSTSIPSSSENSP---LSSSYSIPSSSSDQNLENSSSSLPL-TTNSQLSPKSLLSQSPS-SLSS 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 151 PDHHGLGTDDCLPSRTAQQRVPPGDILYERESRglvKGPLThegnfPCKCGECGKAFNTHGFLVRHEQ--LHSG--VKPY 226
Cdd:COG5048  251 SDSSSSASESPRSSLPTASSQSSSPNESDSSSE---KGFSL-----PIKSKQCNISFSRSSPLTRHLRsvNHSGesLKPF 322

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 227 GCTE--YGRAFSKSTHLLQHHLIPTREKPYECSEC-------GKAFHRRSQLTTHQLIHTGEKPYEC--SECGKGFCDST 295
Cdd:COG5048  323 SCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDS 402

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528993760 296 RLIKHSIIHTGEKPYNC--LECGKAFYRKSYLKEHQRIHTgEKPYVCTECGRAFVYCSTFILHKRA 359
Cdd:COG5048  403 NLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
324-349 3.67e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.67e-05
                          10        20
                  ....*....|....*....|....*.
gi 528993760  324 YLKEHQRIHTGEKPYVCTECGRAFVY 349
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-312 5.92e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 5.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528993760 252 KPYECSECGKAFHRRSQLTTHQLIHTGEKPYECS--ECGKGFCDSTRLIKHSIIHTGEKPYNC 312
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLN 94
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
280-417 6.18e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760 280 KPYECSECGKGFCDSTRLIKHSIIHTGEKPYNCL--ECGKAFYRKSYLKEHQRIHTGEKPYVCT-ECGRAFVYCSTFILH 356
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSkSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528993760 357 KRAHTGEKPYGCKECGKAFSSRSSLSRHFTIHSAEKPYKCTEC-GKAFNRRAYLSSHQRIHS 417
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPA 173
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
376-449 1.19e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528993760 376 SSRSSLSRHFTIHSAEKPYKCTECGKAFNRRAYLSSHQRIHSGEKPYTC--VECRKTFWWSSSLVRHSIIHTGEKP 449
Cdd:COG5048   16 LSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
zf-H2C2_2 pfam13465
Zinc-finger double domain;
380-405 3.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.18e-04
                          10        20
                  ....*....|....*....|....*.
gi 528993760  380 SLSRHFTIHSAEKPYKCTECGKAFNR 405
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 52-175 1.61e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760   52 PEPDLISPVEPGPESQTSGSGPTPSSCSGDNTKPETPQPAPSHPAPSEEVSPQKRPSQRASGHSQLEQTKDADRPLEMRE 131
Cdd:PHA03307  802 LRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRA 881

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528993760  132 GPL-------RPGTGPQGKELPGKVNPDHHGLGTDDC--LPSRTAQQRVPPGD 175
Cdd:PHA03307  882 RPGaaappkaAAAAPPAGAPAPRPRPAPRVKLGPMPPggPDPRGGFRRVPPGD 934
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 1.89e-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: 1.89e-03
                          10        20
                  ....*....|....*....|...
gi 528993760  394 YKCTECGKAFNRRAYLSSHQRIH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
269-291 2.22e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.22e-03
                          10        20
                  ....*....|....*....|...
gi 528993760  269 LTTHQLIHTGEKPYECSECGKGF 291
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 310-332 3.06e-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: 3.06e-03
                          10        20
                  ....*....|....*....|...
gi 528993760  310 YNCLECGKAFYRKSYLKEHQRIH 332
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 254-276 3.24e-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: 3.24e-03
                          10        20
                  ....*....|....*....|...
gi 528993760  254 YECSECGKAFHRRSQLTTHQLIH 276
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-321 3.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 528993760  296 RLIKHSIIHTGEKPYNCLECGKAFYR 321
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
408-432 4.37e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.37e-03
                          10        20
                  ....*....|....*....|....*
gi 528993760  408 YLSSHQRIHSGEKPYTCVECRKTFW 432
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 58-147 5.61e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760   58 SPVEPGPESQTSGSG------PTPSSCSGDNTKPETPQPAPSHPAPSEEVSPQKRPSQRASGHSQLEQTKDADRPlEMRE 131
Cdd:PHA03307  330 SSSSESSRGAAVSPGpspsrsPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDAT-GRFP 408

                          90
                  ....*....|....*.
gi 528993760  132 GPLRPGTGPQGKELPG 147
Cdd:PHA03307  409 AGRPRPSPLDAGAASG 424
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 45-114 5.90e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 38.83  E-value: 5.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528993760  45 VSLGCPLPEPDLI-------SPVEPGPESQ-TSGSGPTPSSCSGDNTKPETPQPAPSHPAPSEEVsPQKRPSQRASGH 114
Cdd:PHA03264 270 PSGGSPAPPGDDRpeakpepGPVEDGAPGReTGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADR-PEGWPSLEAITF 346
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 50-136 8.97e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 38.59  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528993760   50 PLPEPDLISPVEPGPESQTSGSGPTPsscsgdntKPETPQPAPSHPAPSEEVSPQKrPSQRASGHSQLEQTKDADRPLEM 129
Cdd:pfam03154 265 PLPQPSLHGQMPPMPHSLQTGPSHMQ--------HPVPPQPFPLTPQSSQSQVPPG-PSPAAPGQSQQRIHTPPSQSQLQ 335

                          90
                  ....*....|..
gi 528993760  130 -----REGPLRP 136
Cdd:pfam03154 336 sqqppREQPLPP 347
 
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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