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Conserved domains on  [gi|145309330|ref|NP_787068|]
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zinc finger protein 792 [Homo sapiens]

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;
14-74 6.74e-24

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 6.74e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309330    14 VTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASLGLISFRSHIVSQLEMGKEPWV 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
348-592 4.41e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 4.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 348 SRSSNLIQHKRVHTGEKPYECSDCGKFFSQRSNLIHHKRVHTGRSAHECSECgkSFNCNSSLIKHWRVHTGErPYKCNEC 427
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSS-SDSSSSA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 428 GKFFSHI---ASLIQHQIVHTGERPHG-------CGECGKAFSRSSDLMKHQR--VHTGE--RPYECNE--CGKLFSQSS 491
Cdd:COG5048  258 SESPRSSlptASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRND 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 492 SLNSHRRLHTGERPYQC--SECGKFFNQSS------SLNNHRRLHTgERPYEC--SECGKTFRQRSNLRQHLKVHKPDRP 561
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLnneppqSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRP 416

                        250       260       270
                 ....*....|....*....|....*....|...
gi 145309330 562 YEC--SECGKAFNQRPTLIRHQKIHIRERSMEN 592
Cdd:COG5048  417 YNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 6.74e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 6.74e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309330    14 VTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASLGLISFRSHIVSQLEMGKEPWV 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.07e-22

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 89.45  E-value: 3.07e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 145309330   13 CVTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 8.43e-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: 74.12  E-value: 8.43e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 145309330  14 VTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASL 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
348-592 4.41e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 4.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 348 SRSSNLIQHKRVHTGEKPYECSDCGKFFSQRSNLIHHKRVHTGRSAHECSECgkSFNCNSSLIKHWRVHTGErPYKCNEC 427
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSS-SDSSSSA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 428 GKFFSHI---ASLIQHQIVHTGERPHG-------CGECGKAFSRSSDLMKHQR--VHTGE--RPYECNE--CGKLFSQSS 491
Cdd:COG5048  258 SESPRSSlptASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRND 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 492 SLNSHRRLHTGERPYQC--SECGKFFNQSS------SLNNHRRLHTgERPYEC--SECGKTFRQRSNLRQHLKVHKPDRP 561
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLnneppqSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRP 416

                        250       260       270
                 ....*....|....*....|....*....|...
gi 145309330 562 YEC--SECGKAFNQRPTLIRHQKIHIRERSMEN 592
Cdd:COG5048  417 YNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449
zf-H2C2_2 pfam13465
Zinc-finger double domain;
352-377 3.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 145309330  352 NLIQHKRVHTGEKPYECSDCGKFFSQ 377
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-74 6.74e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 94.97  E-value: 6.74e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309330    14 VTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASLGLISFRSHIVSQLEMGKEPWV 74
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 13-54 3.07e-22

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 89.45  E-value: 3.07e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 145309330   13 CVTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 14-53 8.43e-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: 74.12  E-value: 8.43e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 145309330  14 VTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASL 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
348-592 4.41e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 65.49  E-value: 4.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 348 SRSSNLIQHKRVHTGEKPYECSDCGKFFSQRSNLIHHKRVHTGRSAHECSECgkSFNCNSSLIKHWRVHTGErPYKCNEC 427
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSS-SDSSSSA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 428 GKFFSHI---ASLIQHQIVHTGERPHG-------CGECGKAFSRSSDLMKHQR--VHTGE--RPYECNE--CGKLFSQSS 491
Cdd:COG5048  258 SESPRSSlptASSQSSSPNESDSSSEKgfslpikSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRND 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 492 SLNSHRRLHTGERPYQC--SECGKFFNQSS------SLNNHRRLHTgERPYEC--SECGKTFRQRSNLRQHLKVHKPDRP 561
Cdd:COG5048  338 ALKRHILLHTSISPAKEklLNSSSKFSPLLnneppqSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRP 416

                        250       260       270
                 ....*....|....*....|....*....|...
gi 145309330 562 YEC--SECGKAFNQRPTLIRHQKIHIRERSMEN 592
Cdd:COG5048  417 YNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
308-625 3.78e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 308 KPYECCECGKFFSQHSSLVKHRRVHTGESPHVCGDCGKF--FSRSSNLIQHKRVHTGEKPYECSDCGK--FFSQRSNLIH 383
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNSKSLPlsNSKASSSSLS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 384 HKRVHT-------------------------------------GRSAHECSEC------------GKSFNCNSSLIKHWR 414
Cdd:COG5048  112 SSSSNSndnnllsshslppssrdpqlpdllsisnlrnnplpgnNSSSVNTPQSnslhpplpanslSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 415 VHTGERPYKCNECGKFFSHIASLIQHQIVHTGERPHGCGECG----------------------------------KAFS 460
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSqlspksllsqspsslsssdssssasesprsslptASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 461 RSSDLMKHQRVHTGER-PYECNECGKLFSQSSSLNSHRR--LHTGE--RPYQCSE--CGKFFNQSSSLNNHRRLHTGERP 533
Cdd:COG5048  272 SSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 534 YEC--SECGKTFRQRSNLRQHLKVH-----KPDRPYEC--SECGKAFNQRPTLIRHQKIHIRERSMENVLLPCSQHTPEI 604
Cdd:COG5048  352 AKEklLNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRH 431

                        410       420
                 ....*....|....*....|.
gi 145309330 605 SSENRPYQGAVNYKLKLVHPS 625
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSIL 452
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
246-497 1.41e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 246 DFHIALRHNKCCESGDAFNNKSTLVQHQRIHSRERPYECSKCGIFFTYAADLTQHQKVHNRGKPYECCECG------KFF 319
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPrsslptASS 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 320 SQHSSLVKHRRVHTGES-PHVCGDCGKFFSRSSNLIQHKR--VHTGE--KPYEC--SDCGKFFSQRSNLIHHKRVHTGRS 392
Cdd:COG5048  271 QSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSIS 350

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309330 393 AHECSECGKSFNcNSSLIKHWRV-----HTGERPYKCNECGKFFS-------HIASLiqHQIVHTGERPHGC--GECGKA 458
Cdd:COG5048  351 PAKEKLLNSSSK-FSPLLNNEPPqslqqYKDLKNDKKSETLSNSCirnfkrdSNLSL--HIITHLSFRPYNCknPPCSKS 427

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 145309330 459 FSRSSDLMKHQRVHTGERPYECNECGKLFSQSSSLNSHR 497
Cdd:COG5048  428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
352-377 3.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 145309330  352 NLIQHKRVHTGEKPYECSDCGKFFSQ 377
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
464-489 5.89e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 5.89e-04
                          10        20
                  ....*....|....*....|....*.
gi 145309330  464 DLMKHQRVHTGERPYECNECGKLFSQ 489
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
548-573 7.23e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.23e-04
                          10        20
                  ....*....|....*....|....*.
gi 145309330  548 NLRQHLKVHKPDRPYECSECGKAFNQ 573
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 534-556 9.97e-04

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: 36.89  E-value: 9.97e-04
                          10        20
                  ....*....|....*....|...
gi 145309330  534 YECSECGKTFRQRSNLRQHLKVH 556
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
492-517 1.09e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.09e-03
                          10        20
                  ....*....|....*....|....*.
gi 145309330  492 SLNSHRRLHTGERPYQCSECGKFFNQ 517
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
520-545 1.42e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|....*.
gi 145309330  520 SLNNHRRLHTGERPYECSECGKTFRQ 545
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 366-388 2.14e-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: 2.14e-03
                          10        20
                  ....*....|....*....|...
gi 145309330  366 YECSDCGKFFSQRSNLIHHKRVH 388
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 338-360 7.45e-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: 7.45e-03
                          10        20
                  ....*....|....*....|...
gi 145309330  338 HVCGDCGKFFSRSSNLIQHKRVH 360
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 506-528 8.64e-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: 8.64e-03
                          10        20
                  ....*....|....*....|...
gi 145309330  506 YQCSECGKFFNQSSSLNNHRRLH 528
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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