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Conserved domains on  [gi|93004100|ref|NP_940896|]
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zinc finger protein 69 homolog isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
76-136 4.47e-34

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.70  E-value: 4.47e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93004100     76 LTFKDISIDFTQEEWGQLAPAHQNLYREVMLENYSNLVSVGYQLSKPSVISQLEKGEEPWM 136
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
232-515 4.55e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 232 VHSNVIIEQRHHKYDTPTKRNTYKLDLINHPTSYIRTKTYECNICekIFKQPIHLTEHMRIHTGEK--PFRCKECGRAFS 309
Cdd:COG5048 188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSdsSSSASESPRSSL 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 310 QSASLSTHQRIHTGE-------KPFECEECGKAFrHRSSLNQHH---RTHTGE--KPYVCDK--CQKAFSQNISLVQHLR 375
Cdd:COG5048 266 PTASSQSSSPNESDSssekgfsLPIKSKQCNISF-SRSSPLTRHlrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 376 THSGEKPFTCnecgktfrqirHLSEHIRIHTGEKPYactaccktfSHRAYLTHHQRIHTgERPYKC--KECGKAFRQRIH 453
Cdd:COG5048 345 LHTSISPAKE-----------KLLNSSSKFSPLLNN---------EPPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSN 403

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93004100 454 LSNHKTVHTGVKAYECN--RCGKAYRHDSSFKKHQRHHTGEKPYECNECGKaFSYNSSLSRHHE 515
Cdd:COG5048 404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
SCAN super family cl42860
leucine rich region;
3-66 1.43e-03

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 38.44  E-value: 1.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93004100      3 QQLLITLPTEASTWVKLQHPKKAVEGAPLWEDVTKMFEGEALlsQDAEDVKTQRESLEDEVTPG 66
Cdd:smart00431  51 EQFLTILPGELQAWVREHHPESGEEAVTLLEDLERELDEPGQ--QVSAHVHGQEVLLEKMVPLG 112
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
76-136 4.47e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.70  E-value: 4.47e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93004100     76 LTFKDISIDFTQEEWGQLAPAHQNLYREVMLENYSNLVSVGYQLSKPSVISQLEKGEEPWM 136
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 75-116 1.39e-20

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: 84.83  E-value: 1.39e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 93004100    75 LLTFKDISIDFTQEEWGQLAPAHQNLYREVMLENYSNLVSVG 116
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 76-114 2.58e-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: 78.36  E-value: 2.58e-18
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 93004100  76 LTFKDISIDFTQEEWGQLAPAHQNLYREVMLENYSNLVS 114
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
232-515 4.55e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 232 VHSNVIIEQRHHKYDTPTKRNTYKLDLINHPTSYIRTKTYECNICekIFKQPIHLTEHMRIHTGEK--PFRCKECGRAFS 309
Cdd:COG5048 188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSdsSSSASESPRSSL 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 310 QSASLSTHQRIHTGE-------KPFECEECGKAFrHRSSLNQHH---RTHTGE--KPYVCDK--CQKAFSQNISLVQHLR 375
Cdd:COG5048 266 PTASSQSSSPNESDSssekgfsLPIKSKQCNISF-SRSSPLTRHlrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 376 THSGEKPFTCnecgktfrqirHLSEHIRIHTGEKPYactaccktfSHRAYLTHHQRIHTgERPYKC--KECGKAFRQRIH 453
Cdd:COG5048 345 LHTSISPAKE-----------KLLNSSSKFSPLLNN---------EPPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSN 403

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93004100 454 LSNHKTVHTGVKAYECN--RCGKAYRHDSSFKKHQRHHTGEKPYECNECGKaFSYNSSLSRHHE 515
Cdd:COG5048 404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
285-310 2.47e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.47e-05
                          10        20
                  ....*....|....*....|....*.
gi 93004100   285 HLTEHMRIHTGEKPFRCKECGRAFSQ 310
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 354-402 9.35e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 9.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 93004100  354 PYVCDKCQKAFSQNISLVQHLRTHSGEKpfTCNECGKTFRQIRHLSEHI 402
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
SCAN smart00431
leucine rich region;
3-66 1.43e-03

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 38.44  E-value: 1.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93004100      3 QQLLITLPTEASTWVKLQHPKKAVEGAPLWEDVTKMFEGEALlsQDAEDVKTQRESLEDEVTPG 66
Cdd:smart00431  51 EQFLTILPGELQAWVREHHPESGEEAVTLLEDLERELDEPGQ--QVSAHVHGQEVLLEKMVPLG 112
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
76-136 4.47e-34

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 122.70  E-value: 4.47e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93004100     76 LTFKDISIDFTQEEWGQLAPAHQNLYREVMLENYSNLVSVGYQLSKPSVISQLEKGEEPWM 136
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 75-116 1.39e-20

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: 84.83  E-value: 1.39e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 93004100    75 LLTFKDISIDFTQEEWGQLAPAHQNLYREVMLENYSNLVSVG 116
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 76-114 2.58e-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: 78.36  E-value: 2.58e-18
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 93004100  76 LTFKDISIDFTQEEWGQLAPAHQNLYREVMLENYSNLVS 114
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
232-515 4.55e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 232 VHSNVIIEQRHHKYDTPTKRNTYKLDLINHPTSYIRTKTYECNICekIFKQPIHLTEHMRIHTGEK--PFRCKECGRAFS 309
Cdd:COG5048 188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSdsSSSASESPRSSL 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 310 QSASLSTHQRIHTGE-------KPFECEECGKAFrHRSSLNQHH---RTHTGE--KPYVCDK--CQKAFSQNISLVQHLR 375
Cdd:COG5048 266 PTASSQSSSPNESDSssekgfsLPIKSKQCNISF-SRSSPLTRHlrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 376 THSGEKPFTCnecgktfrqirHLSEHIRIHTGEKPYactaccktfSHRAYLTHHQRIHTgERPYKC--KECGKAFRQRIH 453
Cdd:COG5048 345 LHTSISPAKE-----------KLLNSSSKFSPLLNN---------EPPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSN 403

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93004100 454 LSNHKTVHTGVKAYECN--RCGKAYRHDSSFKKHQRHHTGEKPYECNECGKaFSYNSSLSRHHE 515
Cdd:COG5048 404 LSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-513 9.15e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 9.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 268 TKTYECNICEKIFKQPIHLTEHMRIHTGEKPFRCKECGRA--FSQSASLSTHQRIHTGEKPFECEECGKAFRHRSSLNQH 345
Cdd:COG5048  31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 346 HRTHTgekpyvcdkcqkAFSQNISLVQHLRTHSGEKPFTCNECGKTFRQIRHLSEHIRIHTGEKPYACTA--------CC 417
Cdd:COG5048 111 SSSSS------------NSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHpplpanslSK 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 418 KTFSHRAYLTHHQRIHTGERPYKCKECGKAFRQRIHLSNHKTVH------------------------TGVKAYECNRCG 473
Cdd:COG5048 179 DPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENsssslplttnsqlspksllsqspsSLSSSDSSSSAS 258

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 93004100 474 KAYRHDSSFKKHQRHH----------TGEKPYECNECGKAFSYNSSLSRH 513
Cdd:COG5048 259 ESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRH 308
zf-H2C2_2 pfam13465
Zinc-finger double domain;
285-310 2.47e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.47e-05
                          10        20
                  ....*....|....*....|....*.
gi 93004100   285 HLTEHMRIHTGEKPFRCKECGRAFSQ 310
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
313-338 1.25e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.25e-04
                          10        20
                  ....*....|....*....|....*.
gi 93004100   313 SLSTHQRIHTGEKPFECEECGKAFRH 338
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
481-506 1.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.50e-04
                          10        20
                  ....*....|....*....|....*.
gi 93004100   481 SFKKHQRHHTGEKPYECNECGKAFSY 506
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
313-517 1.95e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 313 SLSTHQRIHTGEKPFECEECGKAFRHRSSLNQHHRTHTGEKPYVCDKCQKAFSQNISLVQHLRTHSGEKPFTCNECGKTF 392
Cdd:COG5048 185 SLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSS 264

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 393 RQIRHLSEHIRIHTGE-------KPYACTACCKTFSHRAYLTHHQR--IHTGE--RPYKCKE--CGKAFRQRIHLSNHKT 459
Cdd:COG5048 265 LPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHIL 344

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93004100 460 VHTGVKAYEC-------------NRCGKAYRH------------------------DSSFKKHQRHHTGEKPYECN--EC 500
Cdd:COG5048 345 LHTSISPAKEkllnssskfspllNNEPPQSLQqykdlkndkksetlsnscirnfkrDSNLSLHIITHLSFRPYNCKnpPC 424

                       250
                ....*....|....*..
gi 93004100 501 GKAFSYNSSLSRHHEIH 517
Cdd:COG5048 425 SKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
397-422 3.01e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.01e-04
                          10        20
                  ....*....|....*....|....*.
gi 93004100   397 HLSEHIRIHTGEKPYACTACCKTFSH 422
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
369-394 3.49e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.49e-04
                          10        20
                  ....*....|....*....|....*.
gi 93004100   369 SLVQHLRTHSGEKPFTCNECGKTFRQ 394
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
341-366 4.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.04e-04
                          10        20
                  ....*....|....*....|....*.
gi 93004100   341 SLNQHHRTHTGEKPYVCDKCQKAFSQ 366
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
429-450 4.08e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.08e-04
                          10        20
                  ....*....|....*....|..
gi 93004100   429 HQRIHTGERPYKCKECGKAFRQ 450
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 354-402 9.35e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 39.47  E-value: 9.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 93004100  354 PYVCDKCQKAFSQNISLVQHLRTHSGEKpfTCNECGKTFRQIRHLSEHI 402
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 327-349 1.30e-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: 36.12  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|...
gi 93004100   327 FECEECGKAFRHRSSLNQHHRTH 349
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SCAN smart00431
leucine rich region;
3-66 1.43e-03

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 38.44  E-value: 1.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93004100      3 QQLLITLPTEASTWVKLQHPKKAVEGAPLWEDVTKMFEGEALlsQDAEDVKTQRESLEDEVTPG 66
Cdd:smart00431  51 EQFLTILPGELQAWVREHHPESGEEAVTLLEDLERELDEPGQ--QVSAHVHGQEVLLEKMVPLG 112
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 271-293 5.93e-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: 5.93e-03
                          10        20
                  ....*....|....*....|...
gi 93004100   271 YECNICEKIFKQPIHLTEHMRIH 293
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 299-321 8.04e-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: 33.81  E-value: 8.04e-03
                          10        20
                  ....*....|....*....|...
gi 93004100   299 FRCKECGRAFSQSASLSTHQRIH 321
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 383-405 8.12e-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: 33.81  E-value: 8.12e-03
                          10        20
                  ....*....|....*....|...
gi 93004100   383 FTCNECGKTFRQIRHLSEHIRIH 405
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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