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Conserved domains on  [gi|163644300|ref|NP_940809|]
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uncharacterized protein LOC112415 [Mus musculus]

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
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-75 5.75e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 5.75e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644300    14 VTFRDVAVDFSQEEWACLDATQKVLYRNIMLETYSNLVAvVGRCISKPDLIVLLEQEKEPWM 75
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVS-LGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
226-637 1.38e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 226 KPFQCNECGKAFHLPDLLKYHKVIHTGEKPFECEVCGKFFSRVSSLAEHR------------------IVHADVKPYECS 287
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRhlrthhnnpsdlnskslpLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 288 ECGKAFKRRSDLMQHQKIHSGERPFQCKDCGKAFIVLAQLAQHQSIHTGEKleckhcgKIFSSGFYLVRHQSIHTGEKPF 367
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP-------QSNSLHPPLPANSLSKDPSSNL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 368 GCHVcgkafrlqvylneHQKTHTDEKPFKCKLCGSAFRRKYQLSEHQKIHTNVKPYQCKECGKSFRRRSNFTEHQSIHTG 447
Cdd:COG5048  185 SLLI-------------SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSS 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 448 KKPFECKDCGKVFRLNIHLIR--HQRFHSGK-----TPFECNECGKGFHFSSQLNYHK--TIHTGQ--TPFECKE--CGK 514
Cdd:COG5048  252 DSSSSASESPRSSLPTASSQSssPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGK 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 515 SFKRICSLLEHGVIHAAVKPFEC--SECGKTFNRRSN-----LIQHQKIHSDERPFEC--KDCGKAFTVLAQLTRHHTIH 585
Cdd:COG5048  332 LFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITH 411

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163644300 586 TGKKSYECE--QCGSAFRLPYQLTQHQRIHDDVKPFQCkeCGKGFVRGTALRIH 637
Cdd:COG5048  412 LSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-75 5.75e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 5.75e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644300    14 VTFRDVAVDFSQEEWACLDATQKVLYRNIMLETYSNLVAvVGRCISKPDLIVLLEQEKEPWM 75
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVS-LGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-53 3.71e-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: 86.76  E-value: 3.71e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 163644300   13 SVTFRDVAVDFSQEEWACLDATQKVLYRNIMLETYSNLVAV 53
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-51 1.87e-17

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 76.05  E-value: 1.87e-17
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 163644300  14 VTFRDVAVDFSQEEWACLDATQKVLYRNIMLETYSNLV 51
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
226-637 1.38e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 226 KPFQCNECGKAFHLPDLLKYHKVIHTGEKPFECEVCGKFFSRVSSLAEHR------------------IVHADVKPYECS 287
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRhlrthhnnpsdlnskslpLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 288 ECGKAFKRRSDLMQHQKIHSGERPFQCKDCGKAFIVLAQLAQHQSIHTGEKleckhcgKIFSSGFYLVRHQSIHTGEKPF 367
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP-------QSNSLHPPLPANSLSKDPSSNL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 368 GCHVcgkafrlqvylneHQKTHTDEKPFKCKLCGSAFRRKYQLSEHQKIHTNVKPYQCKECGKSFRRRSNFTEHQSIHTG 447
Cdd:COG5048  185 SLLI-------------SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSS 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 448 KKPFECKDCGKVFRLNIHLIR--HQRFHSGK-----TPFECNECGKGFHFSSQLNYHK--TIHTGQ--TPFECKE--CGK 514
Cdd:COG5048  252 DSSSSASESPRSSLPTASSQSssPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGK 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 515 SFKRICSLLEHGVIHAAVKPFEC--SECGKTFNRRSN-----LIQHQKIHSDERPFEC--KDCGKAFTVLAQLTRHHTIH 585
Cdd:COG5048  332 LFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITH 411

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163644300 586 TGKKSYECE--QCGSAFRLPYQLTQHQRIHDDVKPFQCkeCGKGFVRGTALRIH 637
Cdd:COG5048  412 LSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-321 1.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.85e-03
                          10        20
                  ....*....|....*....|....
gi 163644300  298 DLMQHQKIHSGERPFQCKDCGKAF 321
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-75 5.75e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 117.69  E-value: 5.75e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644300    14 VTFRDVAVDFSQEEWACLDATQKVLYRNIMLETYSNLVAvVGRCISKPDLIVLLEQEKEPWM 75
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVS-LGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-53 3.71e-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: 86.76  E-value: 3.71e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 163644300   13 SVTFRDVAVDFSQEEWACLDATQKVLYRNIMLETYSNLVAV 53
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-51 1.87e-17

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 76.05  E-value: 1.87e-17
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 163644300  14 VTFRDVAVDFSQEEWACLDATQKVLYRNIMLETYSNLV 51
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLV 38
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
226-637 1.38e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 79.74  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 226 KPFQCNECGKAFHLPDLLKYHKVIHTGEKPFECEVCGKFFSRVSSLAEHR------------------IVHADVKPYECS 287
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRhlrthhnnpsdlnskslpLSNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 288 ECGKAFKRRSDLMQHQKIHSGERPFQCKDCGKAFIVLAQLAQHQSIHTGEKleckhcgKIFSSGFYLVRHQSIHTGEKPF 367
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP-------QSNSLHPPLPANSLSKDPSSNL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 368 GCHVcgkafrlqvylneHQKTHTDEKPFKCKLCGSAFRRKYQLSEHQKIHTNVKPYQCKECGKSFRRRSNFTEHQSIHTG 447
Cdd:COG5048  185 SLLI-------------SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSS 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 448 KKPFECKDCGKVFRLNIHLIR--HQRFHSGK-----TPFECNECGKGFHFSSQLNYHK--TIHTGQ--TPFECKE--CGK 514
Cdd:COG5048  252 DSSSSASESPRSSLPTASSQSssPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGK 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 515 SFKRICSLLEHGVIHAAVKPFEC--SECGKTFNRRSN-----LIQHQKIHSDERPFEC--KDCGKAFTVLAQLTRHHTIH 585
Cdd:COG5048  332 LFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITH 411

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163644300 586 TGKKSYECE--QCGSAFRLPYQLTQHQRIHDDVKPFQCkeCGKGFVRGTALRIH 637
Cdd:COG5048  412 LSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLC--SILKSFRRDLDLSN 463
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
391-643 5.42e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 391 DEKPFKCKLCGSAFRRKYQLSEHQKIHTNVKPYQC--KECGKSFRRRSNFTEHQSIHTGKKPFECKDCGK---------- 458
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPlsnskassss 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 459 -------------------------------VFRLNIHLIRHQRFHSGKTPFEC----------NECGKGFHFSSQLNYH 497
Cdd:COG5048  110 lsssssnsndnnllsshslppssrdpqlpdlLSISNLRNNPLPGNNSSSVNTPQsnslhpplpaNSLSKDPSSNLSLLIS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 498 KTIHTGQTPFECKECGKSFKRICSLLEHGVIHAAVKPFECSECGKTFNRRSNLIQHQKIHSDERPFECKDCGKAFTVLAQ 577
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644300 578 LTRHHTIHTG-------KKSYECEQCGSAFRLPYQLTQHQR--IHD--DVKPFQCKE--CGKGFVRGTALRIHQRVHTG 643
Cdd:COG5048  270 SQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSgeSLKPFSCPYslCGKLFSRNDALKRHILLHTS 348
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 224-307 9.75e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.01  E-value: 9.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644300 224 GEKPFQCN--ECGKAFHLPDLLKYHKvIHTGEKPFECEVcgkffsrvSSLAEHRIVHADVKPYECSECGKAFKRRSDLMQ 301
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHM-LHGHQNQKLHEN--------PSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 163644300 302 HQKiHS 307
Cdd:COG5189  417 HRK-HS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
214-237 1.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....
gi 163644300  214 ELTRHQKSHSGEKPFQCNECGKAF 237
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-321 1.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.85e-03
                          10        20
                  ....*....|....*....|....
gi 163644300  298 DLMQHQKIHSGERPFQCKDCGKAF 321
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
243-267 2.53e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.53e-03
                          10        20
                  ....*....|....*....|....*
gi 163644300  243 LKYHKVIHTGEKPFECEVCGKFFSR 267
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
410-434 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 163644300  410 LSEHQKIHTNVKPYQCKECGKSFRR 434
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
494-518 3.64e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 3.64e-03
                          10        20
                  ....*....|....*....|....*
gi 163644300  494 LNYHKTIHTGQTPFECKECGKSFKR 518
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 535-557 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 163644300  535 FECSECGKTFNRRSNLIQHQKIH 557
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 423-445 5.31e-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: 34.58  E-value: 5.31e-03
                          10        20
                  ....*....|....*....|...
gi 163644300  423 YQCKECGKSFRRRSNFTEHQSIH 445
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 284-306 7.13e-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: 7.13e-03
                          10        20
                  ....*....|....*....|...
gi 163644300  284 YECSECGKAFKRRSDLMQHQKIH 306
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
381-406 7.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 7.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 163644300  381 YLNEHQKTHTDEKPFKCKLCGSAFRR 406
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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