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Conserved domains on  [gi|1958669066|ref|XP_038945496|]
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zinc finger protein 157 isoform X1 [Rattus norvegicus]

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;
5-65 9.76e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.54  E-value: 9.76e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669066    5 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLGHCVTKPELILRLEHGFRPWS 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
183-529 2.61e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 183 KIYQCTECRKAFPSKSELTVHHRIHTGEKPHEC--DECGKAFYRKSTLTVHQKTHRGEKPYEC-KECCKAFYYKSTLTEH 259
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 260 QRIHTGEKPYVCKECGKAFFYKSNLTRHHRTHTGEKPYECEEC-RKGFSSKSELTSHHRTHtgekpyQCEECGKAFYCKS 338
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLP------ANSLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 339 TLRVHQKIHTGEKPYECKECQKSFYYKSTLTEH------------QRTHTGEKPY---------------ECKDCGKAFF 391
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQnlensssslpltTNSQLSPKSLlsqspsslsssdsssSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 392 YKSQLTRHHRIHTGE-------KPYECEECRKAFSSKSELTAHHRT--HTGE--KPYECEE--CGKCFCRKSHLTLHHRI 458
Cdd:COG5048   266 PTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669066 459 HTGEKPYECKdcrkaffcksgLARHLGTHTHGTNTKNREKHFPATQSSVNIRNDTQVRNPVAIKNEEKHST 529
Cdd:COG5048   346 HTSISPAKEK-----------LLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLS 405
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
5-65 9.76e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.54  E-value: 9.76e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669066    5 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLGHCVTKPELILRLEHGFRPWS 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 4-45 6.04e-23

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: 91.38  E-value: 6.04e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958669066   4 LVSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLG 45
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 5-44 1.09e-19

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: 82.21  E-value: 1.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958669066   5 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSL 44
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
183-529 2.61e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 183 KIYQCTECRKAFPSKSELTVHHRIHTGEKPHEC--DECGKAFYRKSTLTVHQKTHRGEKPYEC-KECCKAFYYKSTLTEH 259
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 260 QRIHTGEKPYVCKECGKAFFYKSNLTRHHRTHTGEKPYECEEC-RKGFSSKSELTSHHRTHtgekpyQCEECGKAFYCKS 338
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLP------ANSLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 339 TLRVHQKIHTGEKPYECKECQKSFYYKSTLTEH------------QRTHTGEKPY---------------ECKDCGKAFF 391
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQnlensssslpltTNSQLSPKSLlsqspsslsssdsssSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 392 YKSQLTRHHRIHTGE-------KPYECEECRKAFSSKSELTAHHRT--HTGE--KPYECEE--CGKCFCRKSHLTLHHRI 458
Cdd:COG5048   266 PTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669066 459 HTGEKPYECKdcrkaffcksgLARHLGTHTHGTNTKNREKHFPATQSSVNIRNDTQVRNPVAIKNEEKHST 529
Cdd:COG5048   346 HTSISPAKEK-----------LLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLS 405
zf-H2C2_2 pfam13465
Zinc-finger double domain;
283-308 6.86e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.86e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958669066 283 NLTRHHRTHTGEKPYECEECRKGFSS 308
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
5-65 9.76e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 116.54  E-value: 9.76e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669066    5 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLGHCVTKPELILRLEHGFRPWS 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 4-45 6.04e-23

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: 91.38  E-value: 6.04e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958669066   4 LVSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSLG 45
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 5-44 1.09e-19

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: 82.21  E-value: 1.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958669066   5 VSFEDVAVDFTWQEWQELDAAQRTLYRDVMLENYSSLVSL 44
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
183-529 2.61e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 183 KIYQCTECRKAFPSKSELTVHHRIHTGEKPHEC--DECGKAFYRKSTLTVHQKTHRGEKPYEC-KECCKAFYYKSTLTEH 259
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNsKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 260 QRIHTGEKPYVCKECGKAFFYKSNLTRHHRTHTGEKPYECEEC-RKGFSSKSELTSHHRTHtgekpyQCEECGKAFYCKS 338
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLP------ANSLSKDPSSNLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 339 TLRVHQKIHTGEKPYECKECQKSFYYKSTLTEH------------QRTHTGEKPY---------------ECKDCGKAFF 391
Cdd:COG5048   186 LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQnlensssslpltTNSQLSPKSLlsqspsslsssdsssSASESPRSSL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 392 YKSQLTRHHRIHTGE-------KPYECEECRKAFSSKSELTAHHRT--HTGE--KPYECEE--CGKCFCRKSHLTLHHRI 458
Cdd:COG5048   266 PTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669066 459 HTGEKPYECKdcrkaffcksgLARHLGTHTHGTNTKNREKHFPATQSSVNIRNDTQVRNPVAIKNEEKHST 529
Cdd:COG5048   346 HTSISPAKEK-----------LLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLS 405
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
267-423 3.89e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 3.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 267 KPYVCKECGKAFFYKSNLTRHHRT--HTGE--KPYECEE--CRKGFSSKSELTSHHRTHTGEKPYQCEEC-------GKA 333
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 334 FYCKSTLRVHQKIHTGEKPYEC--KECQKSFYYKSTLTEHQRTHTGEKPYECKD--CGKAFFYKSQLTRHHRIHTGEKPY 409
Cdd:COG5048   368 NNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPL 447

                         170
                  ....*....|....
gi 1958669066 410 ECEECRKAFSSKSE 423
Cdd:COG5048   448 LCSILKSFRRDLDL 461
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
435-557 2.97e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 435 KPYECEECGKCFCRKSHLTLHHRIHTGEKPYECKDCRKAFFCKSGLARHLGTHTHGTNTKNREKH--------------- 499
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKslplsnskassssls 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 500 ----------FPATQSSVNIRNDTQVRNPVAIKN--EEKHSTINQSSVHMMDFLELRSPIDVHNAGKLAF 557
Cdd:COG5048   112 ssssnsndnnLLSSHSLPPSSRDPQLPDLLSISNlrNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPS 181
zf-H2C2_2 pfam13465
Zinc-finger double domain;
283-308 6.86e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.86e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958669066 283 NLTRHHRTHTGEKPYECEECRKGFSS 308
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
396-420 8.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.43e-04
                          10        20
                  ....*....|....*....|....*
gi 1958669066 396 LTRHHRIHTGEKPYECEECRKAFSS 420
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
155-344 9.65e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 155 KPYEWKECQKAFCYKSALTQHQRprtrlkiyqctecrkafpskseltvhHRIHTGE--KPHECDE--CGKAFYRKSTLTV 230
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLR--------------------------SVNHSGEslKPFSCPYslCGKLFSRNDALKR 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669066 231 HQKTHRGEKPYECK--ECCKAF-----YYKSTLTEHQRIHTGEKPYVC--KECGKAFFYKSNLTRHHRTHTGEKPYECE- 300
Cdd:COG5048   342 HILLHTSISPAKEKllNSSSKFspllnNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKn 421

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958669066 301 -ECRKGFSSKSELTSHHRTHTGEKPYQCEECGKAFYCKSTLRVHQ 344
Cdd:COG5048   422 pPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
311-336 1.50e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.50e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958669066 311 ELTSHHRTHTGEKPYQCEECGKAFYC 336
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-390 1.55e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|...
gi 1958669066 368 LTEHQRTHTGEKPYECKDCGKAF 390
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-364 1.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*
gi 1958669066 340 LRVHQKIHTGEKPYECKECQKSFYY 364
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
256-278 1.92e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.92e-03
                          10        20
                  ....*....|....*....|...
gi 1958669066 256 LTEHQRIHTGEKPYVCKECGKAF 278
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 437-459 2.78e-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: 2.78e-03
                          10        20
                  ....*....|....*....|...
gi 1958669066 437 YECEECGKCFCRKSHLTLHHRIH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
199-224 2.96e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.96e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958669066 199 ELTVHHRIHTGEKPHECDECGKAFYR 224
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 269-291 3.70e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 3.70e-03
                          10        20
                  ....*....|....*....|...
gi 1958669066 269 YVCKECGKAFFYKSNLTRHHRTH 291
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 381-403 7.64e-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: 7.64e-03
                          10        20
                  ....*....|....*....|...
gi 1958669066 381 YECKDCGKAFFYKSQLTRHHRIH 403
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
451-474 8.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 8.07e-03
                          10        20
                  ....*....|....*....|....
gi 1958669066 451 HLTLHHRIHTGEKPYECKDCRKAF 474
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
423-446 8.64e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 8.64e-03
                          10        20
                  ....*....|....*....|....
gi 1958669066 423 ELTAHHRTHTGEKPYECEECGKCF 446
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
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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